B Number Gene Name Strand Orientation Protein Length Mrna

Total Page:16

File Type:pdf, Size:1020Kb

B Number Gene Name Strand Orientation Protein Length Mrna list list sample) short list predicted B number Operon ID Gene name assignment Protein length mRNA present mRNA intensity Gene description Protein detected - Strand orientation Membrane protein detected (total list) detected (long list) membrane sample Proteins detected - detected (short list) # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides Functional category detected (membrane Protein detected - total Protein detected - long b0001 thrL + 21 1344 P 1 0 0 0 0 thr operon leader peptide Metabolism of small molecules 1 b0002 thrA + 820 13624 P 39 P 18 P 18 P 18 P(m) 2 aspartokinase I, homoserine dehydrogenase I Metabolism of small molecules 1 b0003 thrB + 310 6781 P 9 P 3 3 P 3 0 homoserine kinase Metabolism of small molecules 1 b0004 thrC + 428 15039 P 18 P 10 P 11 P 10 0 threonine synthase Metabolism of small molecules 1 b0005 b0005 + 98 432 A 5 0 0 0 0 orf, hypothetical protein Open reading frames 2 b0006 yaaA - 258 1047 P 11 P 1 2 P 1 0 orf, hypothetical protein Open reading frames 3 b0007 yaaJ - 476 342 P 8 0 0 0 0 MP-GenProt-PHD inner membrane transport protein Miscellaneous 4 b0008 talB + 317 20561 P 20 P 13 P 16 P 13 0 transaldolase B Metabolism of small molecules 5 b0009 mog + 195 1296 P 7 0 0 0 0 required for the efficient incorporation of molybdate into molybdoproteins Metabolism of small molecules 6 b0010 yaaH - 188 407 A 2 0 0 0 0 PHD orf, hypothetical protein Open reading frames 7 b0011 b0011 - 237 338 P 13 0 0 0 0 putative oxidoreductase Miscellaneous 8 b0012 htgA + 196 149 P 11 0 0 0 0 positive regulator for sigma 32 heat shock promoters Cell processes 9 b0013 yaaI - 134 288 A 7 0 0 0 0 orf, hypothetical protein Open reading frames 10 b0014 dnaK + 638 13283 P 32 P 23 P 24 P 23 0 chaperone Hsp70; DNA biosynthesis; autoregulated heat shock proteins Cell processes 11 b0015 dnaJ + 376 4492 P 13 P 4 P 6 P 4 P(m) 1 chaperone with DnaK; heat shock protein Cell processes 11 b0016 yi81_1 + 370 17 0 0 0 0 IS186 hypothetical protein Extrachromosomal 12 b0017 yi82_1 - 102 135 P 6 0 0 0 0 IS186 and IS421 hypothetical protein Extrachromosomal 13 b0018 gef - 69 215 P 3 0 0 0 0 Gef protein interferes with membrane function when in excess Cell processes 14 b0019 nhaA + 388 1174 P 7 0 0 0 0 GenProt-PHD Na+/H antiporter, pH dependent Cell processes 15 b0020 nhaR + 301 645 P 13 0 0 0 0 transcriptional activator of nhaA Cell processes 16 b0021 insB_1 - 167 9 0 0 0 0 IS1 protein InsB Extrachromosomal 17 b0022 insA_1 - 91 5 0 0 0 0 IS1 protein InsA Extrachromosomal 17 b0023 rpsT - 87 7837 P 3 P 2 2 P 2 0 30S ribosomal subunit protein S20 Structural elements 18 b0024 b0024 + 72 163 P 4 0 0 0 0 PHD orf, hypothetical protein Open reading frames 19 b0025 ribF + 313 3873 P 15 0 0 0 0 putative regulator Metabolism of small molecules 19 list list sample) short list predicted B number Operon ID Gene name assignment Protein length mRNA present mRNA intensity Gene description Protein detected - Strand orientation Membrane protein detected (total list) detected (long list) membrane sample Proteins detected - detected (short list) # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides Functional category detected (membrane Protein detected - total Protein detected - long b0026 ileS + 938 4036 P 46 P 13 P 14 P 13 0 isoleucine tRNA synthetase Macromolecule metabolism 20 b0027 lspA + 164 3643 P 6 0 0 0 0 GenProt-PHD prolipoprotein signal peptidase (SPase II) Macromolecule metabolism 20 probable FKBX-type 16KD peptidyl-prolyl cis-trans isomerase (a b0028 slpA + 149 2825 P 5 P 1 2 P 1 0 rotamase) Macromolecule metabolism 21 b0029 lytB + 316 1331 P 16 P 2 2 P 2 0 control of stringent response; involved in penicillin tolerance Global functions 20 b0030 yaaF + 304 685 P 8 0 0 0 0 orf, hypothetical protein Open reading frames 22 b0031 dapB + 273 2348 P 16 P 3 3 P 3 0 dihydrodipicolinate reductase Metabolism of small molecules 23 b0032 carA + 382 9312 P 14 P 8 P 8 P 8 0 carbamoyl-phosphate synthetase, glutamine (small) subunit Metabolism of small molecules 24 b0033 carB + 1073 7656 P 48 P 17 P 19 P 17 0 carbamoyl-phosphate synthase large subunit Metabolism of small molecules 24 b0034 caiF + 166 813 P 9 0 0 0 0 transcriptional regulator of cai operon Metabolism of small molecules 25 b0035 caiE - 203 190 P 7 0 0 0 0 possible synthesis of cofactor for carnitine racemase and dehydratase Metabolism of small molecules 26 b0036 caiD - 297 476 P 14 0 0 0 0 carnitine racemase Metabolism of small molecules 26 b0037 caiC - 522 285 P 25 0 0 0 0 GenProt-PHD probable crotonobetaine/carnitine-CoA ligase Metabolism of small molecules 26 b0038 caiB - 405 291 P 19 0 0 0 0 l-carnitine dehydratase Metabolism of small molecules 26 b0039 caiA - 380 308 A 18 0 0 0 0 probable carnitine operon oxidoreductase Metabolism of small molecules 26 b0040 caiT - 504 148 A 5 0 0 0 0 GenProt-PHD probable carnitine transporter Metabolism of small molecules 26 b0041 fixA + 268 105 A 6 0 0 0 0 probable flavoprotein subunit, carnitine metabolism Metabolism of small molecules 27 b0042 fixB + 313 365 P 14 0 0 0 0 probable flavoprotein subunit, carnitine metabolism Metabolism of small molecules 27 b0043 fixC + 428 215 A 19 0 0 0 0 flavoprotein; electron transport Metabolism of small molecules 27 b0044 fixX + 95 135 A 7 0 0 0 0 putative ferredoxin Metabolism of small molecules 27 b0045 yaaU + 443 133 P 7 0 0 0 0 GenProt-PHD putative transport protein Cell processes 28 b0046 yabF + 176 356 P 6 0 0 0 0 putative NAD(P)H oxidoreductase Metabolism of small molecules 29 b0047 kefC + 620 543 P 29 0 0 0 0 GenProt-PHD K+ efflux antiporter, glutathione-regulated Cell processes 29 b0048 folA + 159 1588 P 7 P 1 2 P 1 0 dihydrofolate reductase type I; trimethoprim resistance Metabolism of small molecules 30 b0049 apaH - 280 703 P 11 P 2 1 P 2 0 diadenosine tetraphosphatase Metabolism of small molecules 31 b0050 apaG - 125 2140 P 5 0 0 0 0 orf, hypothetical protein Open reading frames 32 list list sample) short list predicted B number Operon ID Gene name assignment Protein length mRNA present mRNA intensity Gene description Protein detected - Strand orientation Membrane protein detected (total list) detected (long list) membrane sample Proteins detected - detected (short list) # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides Functional category detected (membrane Protein detected - total Protein detected - long b0051 ksgA - 273 2240 P 10 P 1 2 P 1 0 S-adenosylmethionine-6-N',N'-adenosyl (rRNA) dimethyltransferase Cell processes 32 b0052 pdxA - 329 1543 P 13 0 0 0 0 pyridoxine biosynthesis Metabolism of small molecules 32 peptidyl-prolyl cis-trans isomerase (PPIase), involved in maturation of b0053 surA - 428 3825 P 19 P 4 P 5 P 4 P(m) 1 GenProt outer membrane proteins (1st module) Cell processes 32 b0054 imp - 784 2737 P 42 P 5 0 0 P(m) 5 GenProt organic solvent tolerance Cell processes 33 b0055 yabH + 271 797 P 16 0 0 0 0 putative DNA binding protein Miscellaneous 34 b0056 yabP + 216 470 P 12 0 0 0 0 orf, hypothetical protein Open reading frames 35 b0057 yabQ + 52 327 P 3 0 0 0 0 orf, hypothetical protein Open reading frames 35 b0058 yabO - 219 525 P 8 0 0 0 0 orf, hypothetical protein Macromolecule metabolism 36 b0059 hepA - 968 1379 P 44 P 2 2 P 2 0 probable ATP-dependent RNA helicase Macromolecule metabolism 36 b0060 polB - 783 350 P 40 0 0 0 0 DNA polymerase II Macromolecule metabolism 37 b0061 araD - 231 571 P 8 0 0 0 0 L-ribulose-5-phosphate 4-epimerase Metabolism of small molecules 38 b0062 araA - 500 268 P 17 0 0 0 0 L-arabinose isomerase Metabolism of small molecules 38 b0063 araB - 566 307 P 20 0 0 0 0 L-ribulokinase Metabolism of small molecules 38 b0064 araC + 292 704 P 10 0 0 0 0 transcriptional regulator for ara operon Metabolism of small molecules 39 b0065 yabI + 254 396 A 6 0 0 0 0 PHD orf, hypothetical protein Open reading frames 40 b0066 yabJ - 232 458 P 12 0 0 0 0 putative ATP-binding component of a transport system Cell processes 41 b0067 yabK - 536 774 P 14 0 0 0 0 GenProt-PHD putative transport system permease protein Cell processes 41 b0068 tbpA - 327 957 P 13 P 1 1 P 1 0 thiamin-binding periplasmic protein Cell processes 41 b0069 yabN - 551 472 P 27 0 0 0 0 putative transport protein Cell processes 42 b0070 setA + 392 218 A 7 0 0 0 0 GenProt-PHD Sugar efflux protein Cell processes 43 b0071 leuD - 201 4770 P 10 P 9 P 7 P 9 0 isopropylmalate isomerase subunit Metabolism of small molecules 44 b0072 leuC - 466 10437 P 18 P 9 P 7 P 9 0 3-isopropylmalate isomerase (dehydratase) subunit Metabolism of small molecules 44 b0073 leuB - 364 10273 P 12 P 8 P 8 P 8 0 3-isopropylmalate dehydrogenase Metabolism of small molecules 44 b0074 leuA - 523 11143 P 28 P 7 P 7 P 7 0 2-isopropylmalate synthase Metabolism of small molecules 44 b0075 leuL - 28 1458 P 1 0 0 0 0 leu operon leader peptide Metabolism of small molecules 44 list list sample) short list predicted B number Operon ID Gene name assignment Protein length mRNA present mRNA intensity Gene description Protein detected - Strand orientation Membrane protein detected (total list) detected (long list) membrane sample Proteins detected - detected (short list) # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides # of tryptic peptides Functional category detected (membrane Protein detected - total Protein detected - long b0076 leuO + 373 158 P 15 0 0 0 0 probable transcriptional activator for leuABCD operon Metabolism of small molecules
Recommended publications
  • Transcripts of the Adeno-Associated Virus Genome: Mapping of the Major Rnas MICHAEL R
    JOURNAL OF VIROLOGY, Oct. 1980, p. 79-92 Vol. 36, No. 1 0022-538X/80/10-0079/14$02.00/0 Transcripts of the Adeno-Associated Virus Genome: Mapping of the Major RNAs MICHAEL R. GREEN AND ROBERT G. ROEDER Departments ofBiological Chemistry and Genetics, Division ofBiology and Biomedical Sciences, Washington University School ofMedicine, St. Louis, Missouri 63110 The four major adeno-associated virus type 2 (AAV2)-specific RNAs were mapped on the linear viral genome by a variety of biochemical techniques, including Si nuclease and exonuclease VII mapping, RNA gel-transfer hybridi- zation, and analysis of reverse transcriptase extension products. All the major AAV2 RNAs were derived from the minus DNA strand and had 3' termini at position 96. The nucleus-specific 4.3- and 3.6-kilobase (kb) RNAs had 5' termini at positions 6 and 19, respectively. The 5' terminus of the 2.6-kb RNA mapped to position 38.5. The predominant 2.3-kb AAV2 mRNA was spliced and contained a short leader sequence (approximately 50 nucleotides) which mapped to position 38.5, coincident with the 5' terminus of the 2.6-kb RNA. The 5' end of the body of the 2.3-kb RNA mapped to position 46.5. These results are discussed in terms of the involvement of single versus multiple promoters (for transcription) and RNA splicing mechanisms in the generation of the AAV2 RNAs. Mammalian DNA viruses have provided pow- In our earlier studies ofAAV2 (19), we defined erful models for the analysis and formulation of and partially characterized four predominant mechaisms of gene expression in eucaryotic AAV2 RNAs in virus-infected cells, indicating cells.
    [Show full text]
  • Part One Amino Acids As Building Blocks
    Part One Amino Acids as Building Blocks Amino Acids, Peptides and Proteins in Organic Chemistry. Vol.3 – Building Blocks, Catalysis and Coupling Chemistry. Edited by Andrew B. Hughes Copyright Ó 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ISBN: 978-3-527-32102-5 j3 1 Amino Acid Biosynthesis Emily J. Parker and Andrew J. Pratt 1.1 Introduction The ribosomal synthesis of proteins utilizes a family of 20 a-amino acids that are universally coded by the translation machinery; in addition, two further a-amino acids, selenocysteine and pyrrolysine, are now believed to be incorporated into proteins via ribosomal synthesis in some organisms. More than 300 other amino acid residues have been identified in proteins, but most are of restricted distribution and produced via post-translational modification of the ubiquitous protein amino acids [1]. The ribosomally encoded a-amino acids described here ultimately derive from a-keto acids by a process corresponding to reductive amination. The most important biosynthetic distinction relates to whether appropriate carbon skeletons are pre-existing in basic metabolism or whether they have to be synthesized de novo and this division underpins the structure of this chapter. There are a small number of a-keto acids ubiquitously found in core metabolism, notably pyruvate (and a related 3-phosphoglycerate derivative from glycolysis), together with two components of the tricarboxylic acid cycle (TCA), oxaloacetate and a-ketoglutarate (a-KG). These building blocks ultimately provide the carbon skeletons for unbranched a-amino acids of three, four, and five carbons, respectively. a-Amino acids with shorter (glycine) or longer (lysine and pyrrolysine) straight chains are made by alternative pathways depending on the available raw materials.
    [Show full text]
  • Adaptive Laboratory Evolution Enhances Methanol Tolerance and Conversion in Engineered Corynebacterium Glutamicum
    ARTICLE https://doi.org/10.1038/s42003-020-0954-9 OPEN Adaptive laboratory evolution enhances methanol tolerance and conversion in engineered Corynebacterium glutamicum Yu Wang 1, Liwen Fan1,2, Philibert Tuyishime1, Jiao Liu1, Kun Zhang1,3, Ning Gao1,3, Zhihui Zhang1,3, ✉ ✉ 1234567890():,; Xiaomeng Ni1, Jinhui Feng1, Qianqian Yuan1, Hongwu Ma1, Ping Zheng1,2,3 , Jibin Sun1,3 & Yanhe Ma1 Synthetic methylotrophy has recently been intensively studied to achieve methanol-based biomanufacturing of fuels and chemicals. However, attempts to engineer platform micro- organisms to utilize methanol mainly focus on enzyme and pathway engineering. Herein, we enhanced methanol bioconversion of synthetic methylotrophs by improving cellular tolerance to methanol. A previously engineered methanol-dependent Corynebacterium glutamicum is subjected to adaptive laboratory evolution with elevated methanol content. Unexpectedly, the evolved strain not only tolerates higher concentrations of methanol but also shows improved growth and methanol utilization. Transcriptome analysis suggests increased methanol con- centrations rebalance methylotrophic metabolism by down-regulating glycolysis and up- regulating amino acid biosynthesis, oxidative phosphorylation, ribosome biosynthesis, and parts of TCA cycle. Mutations in the O-acetyl-L-homoserine sulfhydrylase Cgl0653 catalyzing formation of L-methionine analog from methanol and methanol-induced membrane-bound transporter Cgl0833 are proven crucial for methanol tolerance. This study demonstrates the importance of
    [Show full text]
  • Contig Protein Description Symbol Anterior Posterior Ratio
    Table S2. List of proteins detected in anterior and posterior intestine pooled samples. Data on protein expression are mean ± SEM of 4 pools fed the experimental diets. The number of the contig in the Sea Bream Database (http://nutrigroup-iats.org/seabreamdb) is indicated. Contig Protein Description Symbol Anterior Posterior Ratio Ant/Pos C2_6629 1,4-alpha-glucan-branching enzyme GBE1 0.88±0.1 0.91±0.03 0.98 C2_4764 116 kDa U5 small nuclear ribonucleoprotein component EFTUD2 0.74±0.09 0.71±0.05 1.03 C2_299 14-3-3 protein beta/alpha-1 YWHAB 1.45±0.23 2.18±0.09 0.67 C2_268 14-3-3 protein epsilon YWHAE 1.28±0.2 2.01±0.13 0.63 C2_2474 14-3-3 protein gamma-1 YWHAG 1.8±0.41 2.72±0.09 0.66 C2_1017 14-3-3 protein zeta YWHAZ 1.33±0.14 4.41±0.38 0.30 C2_34474 14-3-3-like protein 2 YWHAQ 1.3±0.11 1.85±0.13 0.70 C2_4902 17-beta-hydroxysteroid dehydrogenase 14 HSD17B14 0.93±0.05 2.33±0.09 0.40 C2_3100 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 ABHD5 0.85±0.07 0.78±0.13 1.10 C2_15440 1-phosphatidylinositol phosphodiesterase PLCD1 0.65±0.12 0.4±0.06 1.65 C2_12986 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1 PLCD1 0.76±0.08 1.15±0.16 0.66 C2_4412 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 PLCG2 1.13±0.08 2.08±0.27 0.54 C2_3170 2,4-dienoyl-CoA reductase, mitochondrial DECR1 1.16±0.1 0.83±0.03 1.39 C2_1520 26S protease regulatory subunit 10B PSMC6 1.37±0.21 1.43±0.04 0.96 C2_4264 26S protease regulatory subunit 4 PSMC1 1.2±0.2 1.78±0.08 0.68 C2_1666 26S protease regulatory subunit 6A PSMC3 1.44±0.24 1.61±0.08
    [Show full text]
  • Ubc 2008 Spring Li Alice.Pdf
    IDENTIFICATION OF VIRULENCE DETERMINANTS OF MYCOBACTERIUM TUBERCULOSIS VIA GENETIC COMPARISONS OF A VIRULENT AND AN ATTENUATED STRAIN OF MYCOBACTERIUM TUBERCULOSIS. by ALICE HOY LAM LI B.Sc., The University of British Columbia, 2001 A THESIS SUBMITTED IN PARTIAL FULFILLMENT OF THE REQUIRMENT FOR THE DEGREE OF DOCTOR OF PHILOSOPHY in THE FACULTY OF GRADUATE STUDIES (Pathology) THE UNIVERSITY OF BRITISH COLUMBIA (Vancouver) MARCH 2008 Alice Hoy Lam Li, 2008 i ABSTRACT Candidate virulence genes were sought through the genetic analyses of two strains of Mycobacterium tuberculosis, one virulent, H37Rv, one attenuated, H37Ra. Derived from the same parent, H37, genomic differences between strains were first examined via two-dimensional DNA technologies: two-dimensional bacterial genome display, and bacterial comparative genomic hybridisation. The two-dimensional technologies were optimised for mycobacterial use, but failed to yield reproducible genomic differences between the two strains. Expression differences between strains during their infection of murine bone-marrow-derived macrophages were then assessed using Bacterial Artificial Chromosome Fingerprint Arrays. This technique successfully identified expression differences between intracellular M. tuberculosis H37Ra and H37Rv, and six candidate genes were confirmed via quantitative real-time PCR for their differential expression at 168 hours post-infection. Genes identified to be upregulated in the attenuated H37Ra were frdB, frdC, and frdD. Genes upregulated in the virulent H37Rv were pks2, aceE, and Rv1571. Further qPCR analysis of these genes at 4 and 96h post-infection revealed that the frd operon (encoding for the fumarate reductase enzyme complex or FRD) was expressed at higher levels in the virulent H37Rv at earlier time points while the expression of aceE and pks2 was higher in the virulent strain throughout the course of infection.
    [Show full text]
  • Yeast Genome Gazetteer P35-65
    gazetteer Metabolism 35 tRNA modification mitochondrial transport amino-acid metabolism other tRNA-transcription activities vesicular transport (Golgi network, etc.) nitrogen and sulphur metabolism mRNA synthesis peroxisomal transport nucleotide metabolism mRNA processing (splicing) vacuolar transport phosphate metabolism mRNA processing (5’-end, 3’-end processing extracellular transport carbohydrate metabolism and mRNA degradation) cellular import lipid, fatty-acid and sterol metabolism other mRNA-transcription activities other intracellular-transport activities biosynthesis of vitamins, cofactors and RNA transport prosthetic groups other transcription activities Cellular organization and biogenesis 54 ionic homeostasis organization and biogenesis of cell wall and Protein synthesis 48 plasma membrane Energy 40 ribosomal proteins organization and biogenesis of glycolysis translation (initiation,elongation and cytoskeleton gluconeogenesis termination) organization and biogenesis of endoplasmic pentose-phosphate pathway translational control reticulum and Golgi tricarboxylic-acid pathway tRNA synthetases organization and biogenesis of chromosome respiration other protein-synthesis activities structure fermentation mitochondrial organization and biogenesis metabolism of energy reserves (glycogen Protein destination 49 peroxisomal organization and biogenesis and trehalose) protein folding and stabilization endosomal organization and biogenesis other energy-generation activities protein targeting, sorting and translocation vacuolar and lysosomal
    [Show full text]
  • Roles of Amino Acids in the <Italic>Escherichia Coli</Italic
    Article pubs.acs.org/biochemistry Roles of Amino Acids in the Escherichia coli Octaprenyl Diphosphate Synthase Active Site Probed by Structure-Guided Site-Directed Mutagenesis † ∥ † ‡ § † ‡ Keng-Ming Chang, Shih-Hsun Chen, Chih-Jung Kuo, , Chi-Kang Chang, Rey-Ting Guo, , ∥ † ‡ § Jinn-Moon Yang, and Po-Huang Liang*, , , † Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan ‡ Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan § Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan ∥ Department of Biological Science and Technology, National Chiao Tung University, Hsin-Chu 300, Taiwan *S Supporting Information ABSTRACT: Octaprenyl diphosphate synthase (OPPS) catalyzes consecutive condensation reactions of farnesyl diphosphate (FPP) with five molecules of isopentenyl diphosphates (IPP) to generate C40 octaprenyl diphosphate, which constitutes the side chain of ubiquinone or menaquinone. To understand the roles of active site amino acids in substrate binding and catalysis, we conducted site- directed mutagenesis studies with Escherichia coli OPPS. In conclusion, D85 is the most important residue in the first DDXXD motif for both FPP and IPP binding through an H-bond network involving R93 and R94, respectively, whereas R94, K45, R48, and H77 are responsible for IPP binding by providing H-bonds and ionic interactions. K170 and T171 may stabilize the farnesyl carbocation intermediate to facilitate the reaction, whereas R93 and K225 may stabilize the catalytic base (MgPPi) for HR proton abstraction after IPP condensation. K225 and K235 in a flexible loop may interact with FPP when the enzyme becomes a closed conformation, which is therefore crucial for catalysis. Q208 is near the hydrophobic part of IPP and is important for IPP binding and catalysis.
    [Show full text]
  • Curriculum Vitae Vern Lee Schramm
    September 2011 CURRICULUM VITAE VERN LEE SCHRAMM Department of Biochemistry Albert Einstein College of Medicine of Yeshiva University 1300 Morris Park Avenue Bronx, New York 10461 Phone: (718) 430-2813 Fax: (718) 430-8565 E-mail: [email protected] Personal Information: Date of Birth: November 9, 1941 Place of Birth: Howard, South Dakota Citizenship: U.S.A. Home Address: 68 Hampton Oval New Rochelle, NY 10805 Home Telephone: (914) 576-2578 Education: Sept 1959 – June 1963 B.S. in Bacteriology (chemistry emphasis), South Dakota State College Sept 1963 – June 1965 Masters Degree in Nutrition (biochemistry emphasis), Harvard University Research Advisor, Dr. R.P. Geyer Oct 1965 – April 1969 Ph.D. in Mechanism of Enzyme Action, Department of Biochemistry, Australian National University Research Advisor, Dr. John Morrison Postdoctoral Experience: Aug 1969 – Aug 1971 NRC-NSF Postdoctoral Research Associate at NASA Ames Research Center, Biological Adaptation Branch Appointments: July 1999 – Present University Professor of the Albert Einstein College of Medicine July 1995 – Present Ruth Merns Endowed Chair of Biochemistry Aug 1987 – Present Professor and Chairman, Department of Biochemistry, Albert Einstein College of Medicine July 1981 - July 1987 Professor of Biochemistry, Temple University School of Medicine July 1976 - June 1981 Associate Professor of Biochemistry, Temple University School of Medicine Aug 1971 - July 1976 Assistant Professor of Biochemistry, Temple University School of Medicine Vern L. Schramm 2 Fields of Interest: Enzymatic
    [Show full text]
  • Generate Metabolic Map Poster
    Authors: Pallavi Subhraveti Anamika Kothari Quang Ong Ron Caspi An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Ingrid Keseler Peter D Karp Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Csac1394711Cyc: Candidatus Saccharibacteria bacterium RAAC3_TM7_1 Cellular Overview Connections between pathways are omitted for legibility. Tim Holland TM7C00001G0420 TM7C00001G0109 TM7C00001G0953 TM7C00001G0666 TM7C00001G0203 TM7C00001G0886 TM7C00001G0113 TM7C00001G0247 TM7C00001G0735 TM7C00001G0001 TM7C00001G0509 TM7C00001G0264 TM7C00001G0176 TM7C00001G0342 TM7C00001G0055 TM7C00001G0120 TM7C00001G0642 TM7C00001G0837 TM7C00001G0101 TM7C00001G0559 TM7C00001G0810 TM7C00001G0656 TM7C00001G0180 TM7C00001G0742 TM7C00001G0128 TM7C00001G0831 TM7C00001G0517 TM7C00001G0238 TM7C00001G0079 TM7C00001G0111 TM7C00001G0961 TM7C00001G0743 TM7C00001G0893 TM7C00001G0630 TM7C00001G0360 TM7C00001G0616 TM7C00001G0162 TM7C00001G0006 TM7C00001G0365 TM7C00001G0596 TM7C00001G0141 TM7C00001G0689 TM7C00001G0273 TM7C00001G0126 TM7C00001G0717 TM7C00001G0110 TM7C00001G0278 TM7C00001G0734 TM7C00001G0444 TM7C00001G0019 TM7C00001G0381 TM7C00001G0874 TM7C00001G0318 TM7C00001G0451 TM7C00001G0306 TM7C00001G0928 TM7C00001G0622 TM7C00001G0150 TM7C00001G0439 TM7C00001G0233 TM7C00001G0462 TM7C00001G0421 TM7C00001G0220 TM7C00001G0276 TM7C00001G0054 TM7C00001G0419 TM7C00001G0252 TM7C00001G0592 TM7C00001G0628 TM7C00001G0200 TM7C00001G0709 TM7C00001G0025 TM7C00001G0846 TM7C00001G0163 TM7C00001G0142 TM7C00001G0895 TM7C00001G0930 Detoxification Carbohydrate Biosynthesis DNA combined with a 2'- di-trans,octa-cis a 2'- Amino Acid Degradation an L-methionyl- TM7C00001G0190 superpathway of pyrimidine deoxyribonucleotides de novo biosynthesis (E.
    [Show full text]
  • Supplemental Methods
    Supplemental Methods: Sample Collection Duplicate surface samples were collected from the Amazon River plume aboard the R/V Knorr in June 2010 (4 52.71’N, 51 21.59’W) during a period of high river discharge. The collection site (Station 10, 4° 52.71’N, 51° 21.59’W; S = 21.0; T = 29.6°C), located ~ 500 Km to the north of the Amazon River mouth, was characterized by the presence of coastal diatoms in the top 8 m of the water column. Sampling was conducted between 0700 and 0900 local time by gently impeller pumping (modified Rule 1800 submersible sump pump) surface water through 10 m of tygon tubing (3 cm) to the ship's deck where it then flowed through a 156 µm mesh into 20 L carboys. In the lab, cells were partitioned into two size fractions by sequential filtration (using a Masterflex peristaltic pump) of the pre-filtered seawater through a 2.0 µm pore-size, 142 mm diameter polycarbonate (PCTE) membrane filter (Sterlitech Corporation, Kent, CWA) and a 0.22 µm pore-size, 142 mm diameter Supor membrane filter (Pall, Port Washington, NY). Metagenomic and non-selective metatranscriptomic analyses were conducted on both pore-size filters; poly(A)-selected (eukaryote-dominated) metatranscriptomic analyses were conducted only on the larger pore-size filter (2.0 µm pore-size). All filters were immediately submerged in RNAlater (Applied Biosystems, Austin, TX) in sterile 50 mL conical tubes, incubated at room temperature overnight and then stored at -80oC until extraction. Filtration and stabilization of each sample was completed within 30 min of water collection.
    [Show full text]
  • A Novel, Low Power Biosensor for Real Time Monitoring of Creatinine and Urea in Peritoneal Dialysis
    A Novel, Low Power Biosensor for Real Time Monitoring of Creatinine and Urea in Peritoneal Dialysis Bhusana Premanode*, Chris Toumazou** *Department of Bioengineering, Imperial College, London, UK **The Institute of Biomedical Engineering, Imperial College, London, UK ABSTRACT based on the immobilization of urease or creatinase onto the surface of the gate insulator [1]. Novel biosensors, based on immobilized creatininase, The FET-based potentiometric biosensors of creatinine creatinase and urease are developed, using ISFETs with have several disadvantages namely, that there is interference weak inversion at pH 6-8 and 37.0oC. The ISFETs with due to ammonia and other ionic substances [1]. Another circuitry, demonstrate a linear relationship of urea and major drawback is that the response is very non-linear, creatinine at the range of 0-200 mM and 0-20 mM, caused by the fact that the induced changes in pH and respectively. Preliminary results show that biosensors temperature decrease the enzyme activity and stability operating in weak inversion mode can eliminate many of the drastically [2]. Moreover, the devices generate undesired disadvantages of ISFETs operating in the strong inversion extra coulomb charges. region, providing a wide dynamic range output in nanoAmp. Such characteristics fit the analytical requirements for 2 THEORETICAL CONSIDERATIONS improving real-time monitoring in Peritoneal Dialysis (PD). Further work covers stability of ISFET sensors biased with 2.1 Chemical Reactions of Creatinine and Urea CMOS circuits in the weak inversion mode working in the room temperature of 15°C to 40°C. Creatinine and urea are important for diagnosis of renal, thyroid and muscle dysfunctions.
    [Show full text]
  • Structures, Functions, and Mechanisms of Filament Forming Enzymes: a Renaissance of Enzyme Filamentation
    Structures, Functions, and Mechanisms of Filament Forming Enzymes: A Renaissance of Enzyme Filamentation A Review By Chad K. Park & Nancy C. Horton Department of Molecular and Cellular Biology University of Arizona Tucson, AZ 85721 N. C. Horton ([email protected], ORCID: 0000-0003-2710-8284) C. K. Park ([email protected], ORCID: 0000-0003-1089-9091) Keywords: Enzyme, Regulation, DNA binding, Nuclease, Run-On Oligomerization, self-association 1 Abstract Filament formation by non-cytoskeletal enzymes has been known for decades, yet only relatively recently has its wide-spread role in enzyme regulation and biology come to be appreciated. This comprehensive review summarizes what is known for each enzyme confirmed to form filamentous structures in vitro, and for the many that are known only to form large self-assemblies within cells. For some enzymes, studies describing both the in vitro filamentous structures and cellular self-assembly formation are also known and described. Special attention is paid to the detailed structures of each type of enzyme filament, as well as the roles the structures play in enzyme regulation and in biology. Where it is known or hypothesized, the advantages conferred by enzyme filamentation are reviewed. Finally, the similarities, differences, and comparison to the SgrAI system are also highlighted. 2 Contents INTRODUCTION…………………………………………………………..4 STRUCTURALLY CHARACTERIZED ENZYME FILAMENTS…….5 Acetyl CoA Carboxylase (ACC)……………………………………………………………………5 Phosphofructokinase (PFK)……………………………………………………………………….6
    [Show full text]