Supporting Information for Proteomics DOI 10.1002/Pmic.200600568
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De Novo Sequencing and Transcriptome Analysis Reveal Key Genes Regulating Steroid Metabolism in Leaves, Roots, Adventitious Roots and Calli of Periploca Sepium Bunge
ORIGINAL RESEARCH published: 21 April 2017 doi: 10.3389/fpls.2017.00594 De novo Sequencing and Transcriptome Analysis Reveal Key Genes Regulating Steroid Metabolism in Leaves, Roots, Adventitious Roots and Calli of Periploca sepium Bunge Jian Zhang 1, 2, 3, Xinglin Li 1, 3*, Fuping Lu 1, 3, Shanying Wang 1, 3, Yunhe An 4, Xiaoxing Su 4, Xiankuan Li 2, Lin Ma 2 and Guangjian Han 5 1 Key Lab of Industrial Fermentation Microbiology, Tianjin University of Science and Technology, Ministry of Education, Tianjin, China, 2 School of Traditional Chinese Materia Medica, Tianjin University of Traditional Chinese Medicine, Tianjin, China, 3 College of Bioengineering, Tianjin University of Science and Technology, Tianjin, China, 4 Beijing Center for Physical and Chemical Analysis, Beijing, China, 5 Shachuan Biotechnology, Tianjin, China Edited by: Periploca sepium Bunge is a traditional medicinal plant, whose root bark is important Peng Zhang, Institute of Plant Physiology and for Chinese herbal medicine. Its major bioactive compounds are C21 steroids and Ecology, SIBS, CAS, China periplocin, a kind of cardiac glycoside, which are derived from the steroid synthesis Reviewed by: pathway. However, research on P. sepium genome or transcriptomes and their related Kun Yu, genes has been lacking for a long time. In this study we estimated this species Hubei University of Chinese Medicine, China nuclear genome size at 170 Mb (using flow cytometry). Then, RNA sequencing of Jun Yang, four different tissue samples of P. sepium (leaves, roots, adventitious roots, and Shanghai Chenshan Plant Science Research Center (CAS), China calli) was done using the sequencing platform Illumina/Solexa Hiseq 2,500. -
Nuclear PI3K Signaling in Cell Growth and Tumorigenesis
REVIEW published: 13 April 2015 doi: 10.3389/fcell.2015.00024 Nuclear PI3K signaling in cell growth and tumorigenesis William J. Davis, Peter Z. Lehmann and Weimin Li * College of Medical Sciences, Washington State University, Spokane, WA, USA The PI3K/Akt signaling pathway is a major driving force in a variety of cellular functions. Dysregulation of this pathway has been implicated in many human diseases including cancer. While the activity of the cytoplasmic PI3K/Akt pathway has been extensively studied, the functions of these molecules and their effector proteins within the nucleus are poorly understood. Harboring key cellular processes such as DNA replication and repair as well as nascent messenger RNA transcription, the nucleus provides a unique compartmental environment for protein–protein and protein–DNA/RNA interactions required for cell survival, growth, and proliferation. Here we summarize recent advances made toward elucidating the nuclear PI3K/Akt signaling cascade and its key components within the nucleus as they pertain to cell growth and tumorigenesis. This review covers Edited by: the spatial and temporal localization of the major nuclear kinases having PI3K activities Massimo Mattia Santoro, and the counteracting phosphatases as well as the role of nuclear PI3K/Akt signaling in University of Leuven, Belgium mRNA processing and exportation, DNA replication and repair, ribosome biogenesis, cell Reviewed by: Emilio Hirsch, survival, and tumorigenesis. University of Torino, Italy Keywords: nuclear signaling, PI3K/Akt/mTOR, cell growth, tumorigenesis, ribosome biogenesis, cell survival, DNA Andrea Graziani, damage, mRNA processing and export Università VIta-Salute San Raffaele, Italy *Correspondence: Introduction Weimin Li, College of Medical Sciences, Washington State University, 412 E In the late 1970s and early 1980s, the existence of a nuclear phosphatidylinositol (PtdIns) cycle Spokane Falls Blvd., Spokane 99202 was proposed (Manzoli et al., 1978, 1982). -
Structural and Biochemical Characterizations of Three Potential Drug Targets from Pathogens
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology 2020 Structural and Biochemical Characterizations of Three Potential Drug Targets from Pathogens LU LU ACTA UNIVERSITATIS UPSALIENSIS ISSN 1651-6214 ISBN 978-91-513-1148-7 UPPSALA urn:nbn:se:uu:diva-435815 2021 Dissertation presented at Uppsala University to be publicly examined in Room A1:111a, BMC, Husargatan 3, Uppsala, Friday, 16 April 2021 at 13:15 for the degree of Doctor of Philosophy. The examination will be conducted in English. Faculty examiner: Christian Cambillau. Abstract Lu, L. 2021. Structural and Biochemical Characterizations of Three Potential Drug Targets from Pathogens. Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology 2020. 91 pp. Uppsala: Acta Universitatis Upsaliensis. ISBN 978-91-513-1148-7. As antibiotic resistance of various pathogens emerged globally, the need for new effective drugs with novel modes of action became urgent. In this thesis, we focus on infectious diseases, e.g. tuberculosis, malaria, and nosocomial infections, and the corresponding causative pathogens, Mycobacterium tuberculosis, Plasmodium falciparum, and the Gram-negative ESKAPE pathogens that underlie so many healthcare-acquired diseases. Following the same- target-other-pathogen (STOP) strategy, we attempted to comprehensively explore the properties of three promising drug targets. Signal peptidase I (SPase I), existing both in Gram-negative and Gram-positive bacteria, as well as in parasites, is vital for cell viability, due to its critical role in signal peptide cleavage, thus, protein maturation, and secreted protein transport. Three factors, comprising essentiality, a unique mode of action, and easy accessibility, make it an attractive drug target. -
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 -
The Mammalian and Yeast A49 and A34 Heterodimers: Homologous but Not the Same
G C A T T A C G G C A T genes Review The Mammalian and Yeast A49 and A34 Heterodimers: Homologous but Not the Same Rachel McNamar , Katrina Rothblum and Lawrence I. Rothblum * Department of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA; [email protected] (R.M.); [email protected] (K.R.) * Correspondence: [email protected] Abstract: Ribosomal RNA synthesis is the rate-limiting step in ribosome biogenesis. In eukaryotes, RNA polymerase I (Pol I) is responsible for transcribing the ribosomal DNA genes that reside in the nucleolus. Aberrations in Pol I activity have been linked to the development of multiple cancers and other genetic diseases. Therefore, it is key that we understand the mechanisms of Pol I transcription. Recent studies have demonstrated that there are many differences between Pol I transcription in yeast and mammals. Our goal is to highlight the similarities and differences between the polymerase- associated factors (PAFs) in yeast and mammalian cells. We focus on the PAF heterodimer A49/34 in yeast and PAF53/49 in mammals. Recent studies have demonstrated that while the structures between the yeast and mammalian orthologs are very similar, they may function differently during Pol I transcription, and their patterns of regulation are different. Keywords: rRNA transcription; ribosome biogenesis; RNA polymerase I Citation: McNamar, R.; Rothblum, 1. Introduction K.; Rothblum, L.I. The Mammalian Ribosome biogenesis is the process that produces the machinery responsible for syn- and Yeast A49 and A34 Heterodimers: thesizing all the proteins in a cell. This process is extraordinarily complex. -
Extensive Purification of a Putative RNA Polymerase I Holoenzyme
Proc. Natl. Acad. Sci. USA Vol. 94, pp. 11869–11874, October 1997 Biochemistry Extensive purification of a putative RNA polymerase I holoenzyme from plants that accurately initiates rRNA gene transcription in vitro (nucleolusyrDNAygene expression) JULIO SAEZ-VASQUEZ AND CRAIG S. PIKAARD* Biology Department, Washington University, Campus Box 1137, One Brookings Drive, St. Louis, MO 63130 Edited by Masayasu Nomura, University of California, Irvine, CA, and approved August 25, 1997 (received for review May 19, 1997) ABSTRACT RNA polymerase I (pol I) is a nuclear enzyme Encouraged by brief reports that cell-free rRNA gene whose function is to transcribe the duplicated genes encoding transcription could be achieved in plant extracts (22, 23), we set the precursor of the three largest ribosomal RNAs. We report out to develop a cell-free system from broccoli (Brassica a cell-free system from broccoli (Brassica oleracea) inflores- oleracea) to further our studies of rRNA gene regulation in cence that supports promoter-dependent RNA pol I transcrip- Brassica and Arabidopsis (24–28). We show that a pol I- tion in vitro. The transcription system was purified extensively containing activity sufficient for promoter-dependent tran- by DEAE-Sepharose, Biorex 70, Sephacryl S300, and Mono Q scription can be purified extensively, with biochemical prop- chromatography. Activities required for pre-rRNA transcrip- erties suggesting a single complex. Approximately 30 polypep- tion copurified with the polymerase on all four columns, tides are present in fractions purified to near-homogeneity, suggesting their association as a complex. Purified fractions consistent with the estimated mass of the putative holoenzyme programmed transcription initiation from the in vivo start site complex and the expected complexity of the pol I transcription and utilized the same core promoter sequences required in system. -
Sauret-Gü Eto S
Mutations in Escherichia coli aceE and ribB Genes Allow Survival of Strains Defective in the First Step of the Isoprenoid Biosynthesis Pathway Jordi Perez-Gil1, Eva Maria Uros1, Susanna Sauret-Gu¨ eto1¤, L. Maria Lois1, James Kirby2, Minobu Nishimoto2, Edward E. K. Baidoo2, Jay D. Keasling2, Albert Boronat1,3, Manuel Rodriguez- Concepcion1* 1 Centre for Research in Agricultural Genomics (CRAG) CSIC-IRTA-UAB-UB, Campus UAB Bellaterra, Barcelona, Spain, 2 Joint BioEnergy Institute, Emeryville, California, United States of America, 3 Department de Bioquı´mica i Biologia Molecular, Universitat de Barcelona, Barcelona, Spain Abstract A functional 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway is required for isoprenoid biosynthesis and hence survival in Escherichia coli and most other bacteria. In the first two steps of the pathway, MEP is produced from the central metabolic intermediates pyruvate and glyceraldehyde 3-phosphate via 1-deoxy-D-xylulose 5-phosphate (DXP) by the activity of the enzymes DXP synthase (DXS) and DXP reductoisomerase (DXR). Because the MEP pathway is absent from humans, it was proposed as a promising new target to develop new antibiotics. However, the lethal phenotype caused by the deletion of DXS or DXR was found to be suppressed with a relatively high efficiency by unidentified mutations. Here we report that several mutations in the unrelated genes aceE and ribB rescue growth of DXS-defective mutants because the encoded enzymes allowed the production of sufficient DXP in vivo. Together, this work unveils the diversity of mechanisms that can evolve in bacteria to circumvent a blockage of the first step of the MEP pathway. -
Which Distinguish Between RNA Polymerases I and III* (Chromatography on DEAE-Ion-Exchangers/Salt-Activation Profiles/RNA Nucleotidyltransferase) LOREN D
Proc. Nat. Acad. Sci. USA Vol. 73, No. 4, pp. 1029-10&3, April 1976 Biochemistry Transcription in yeast: a-Amanitin sensitivity and other properties which distinguish between RNA polymerases I and III* (chromatography on DEAE-ion-exchangers/salt-activation profiles/RNA nucleotidyltransferase) LOREN D. SCHULTZt AND BENJAMIN D. HALL* t Department of Biochemistry and t'Department of Genetics, University of Washington, Seattle, Wash. 98195 Communicated by Herschel L. Roman, December 29, 1975 ABSTRACT Three peaks of DNA-dependent RNA poly- umns can be interpreted either as a failure of DEAE-cellu- merase (RNA nucleotidyltransferase) activity are resolved by lose to resolve two different enzymes or, alternatively, as the chromatography of a sonicated yeast cell extract on DEAE- Sephadex. The enzymes, which are named RNA polymerases tendency of a single enzyme, polymerase A, to chromato- I, II, and III in order of elution, show similar catalytic prop- graph as two peaks on DEAE-Sephadex as a result of some erties to the vertebrate class I, class II, and class III RNA po- trivial alteration that occurs during the chromatography. lymerases, respectively. Yeast RNA polymerase III is readily For vertebrate RNA polymerases, the first of these interpre- distinguished from yeast polymerase I by its biphasic ammo- tations is the correct one. Sklar, Schwartz, and Roeder (10) nium sulfate activation profile with native DNA templates, have shown, for mouse plasmacytoma RNA polymerases, greater enzymatic activity with poly[d(I-C) than with native that each of the three classes of RNA salmon sperm DNA, and distinctive chromatographic elution polymerase eluted positions from DEAE-cellulose (0.12 M ammonium sulfate) from DEAE-Sephadex has a distinctive pattern of protein compared with DEAE-Sephadex (0.32 M ammonium sulfate). -
The Coordinated Upregulated Expression of Genes Involved In
plants Article The Coordinated Upregulated Expression of Genes Involved in MEP, Chlorophyll, Carotenoid and Tocopherol Pathways, Mirrored the Corresponding Metabolite Contents in Rice Leaves during De-Etiolation Xin Jin 1,2,3,†, Can Baysal 3,†, Margit Drapal 4, Yanmin Sheng 5, Xin Huang 3, Wenshu He 3, Lianxuan Shi 6, Teresa Capell 3, Paul D. Fraser 4, Paul Christou 3,7 and Changfu Zhu 3,5,* 1 Gansu Provincial Key Laboratory of Aridland Crop Science, Gansu Agricultural University, Lanzhou 730070, China; [email protected] 2 College of Life Science and Technology, Gansu Agricultural University, Lanzhou 730070, China 3 Department of Plant Production and Forestry Science, University of Lleida-Agrotecnio CERCA Center, Av. Alcalde Rovira Roure, 191, 25198 Lleida, Spain; [email protected] (C.B.); [email protected] (X.H.); [email protected] (W.H.); [email protected] (T.C.); [email protected] (P.C.) 4 Biochemistry, School of Life Sciences and Environment, Royal Holloway University of London, Egham Hill, Egham, Surrey TW20 0EX, UK; [email protected] (M.D.); [email protected] (P.D.F.) 5 School of Life Sciences, Changchun Normal University, Changchun 130032, China; [email protected] 6 School of Life Sciences, Northeast Normal University, Changchun 130024, China; [email protected] 7 ICREA, Catalan Institute for Research and Advanced Studies, Passeig Lluís Companys 23, 08010 Barcelona, Spain Citation: Jin, X.; Baysal, C.; Drapal, * Correspondence: [email protected] M.; Sheng, Y.; Huang, X.; He, W.; Shi, † These authors contributed equally to this work. L.; Capell, T.; Fraser, P.D.; Christou, P.; et al. -
Evolutionary Diversification and Characterization of the Eubacterial
Carretero-Paulet et al. BMC Evolutionary Biology 2013, 13:180 http://www.biomedcentral.com/1471-2148/13/180 RESEARCH ARTICLE Open Access Evolutionary diversification and characterization of the eubacterial gene family encoding DXR type II, an alternative isoprenoid biosynthetic enzyme Lorenzo Carretero-Paulet1,2*, Agnieszka Lipska1, Jordi Pérez-Gil3, Félix J Sangari4, Victor A Albert1 and Manuel Rodríguez-Concepción3* Abstract Background: Isoprenoids constitute a vast family of natural compounds performing diverse and essential functions in all domains of life. In most eubacteria, isoprenoids are synthesized through the methylerythritol 4-phosphate (MEP) pathway. The production of MEP is usually catalyzed by deoxyxylulose 5-phosphate reductoisomerase (DXR-I) but a few organisms use an alternative DXR-like enzyme (DXR-II). Results: Searches through 1498 bacterial complete proteomes detected 130 sequences with similarity to DXR-II. Phylogenetic analysis identified three well-resolved clades: the DXR-II family (clustering 53 sequences including eleven experimentally verified as functional enzymes able to produce MEP), and two previously uncharacterized NAD(P)-dependent oxidoreductase families (designated DLO1 and DLO2 for DXR-II-like oxidoreductases 1 and 2). Our analyses identified amino acid changes critical for the acquisition of DXR-II biochemical function through type-I functional divergence, two of them mapping onto key residues for DXR-II activity. DXR-II showed a markedly discontinuous distribution, which was verified at several levels: taxonomic (being predominantly found in Alphaproteobacteria and Firmicutes), metabolic (being mostly found in bacteria with complete functional MEP pathways with or without DXR-I), and phenotypic (as no biological/phenotypic property was found to be preferentially distributed among DXR-II-containing strains, apart from pathogenicity in animals). -
Subunits Shared by Eukaryotic Nuclear RNA Polymerases
Downloaded from genesdev.cshlp.org on September 28, 2021 - Published by Cold Spring Harbor Laboratory Press Subunits shared by eukaryotic nuclear RNA polymerases Nancy A. Woychik, Sha-Mei Liao, Peter A. Kolodziej, and Richard A. Young Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142 USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 USA RNA polymerases I, II, and III share three subunits that are immunologically and biochemically indistinguishable. The Saccharomyces cerevisiae genes that encode these subunits (RPBS, RPB6, and RPBS) were isolated and sequenced, and their transcriptional start sites were deduced. RPB5 encodes a 25-kD protein, RPB6, an 18-kD protein, and RPB8, a 16-kD protein. These genes are single copy, reside on different chromosomes, and are essential for viability. The fact that the genes are single copy, corroborates previous evidence suggesting that each of the common subunits is identical in RNA polymerases I, II, and III. Furthermore, immunoprecipitation of RPB6 coprecipitates proteins whose sizes are consistent with RNA polymerase I, II, and III subunits. Sequence similarity between the yeast RPB5 protein and a previously characterized human RNA polymerase subunit demonstrates that the common subunits of the nuclear RNA polymerases are well conserved among eukaryotes. The presence of these conserved and essential subunits in all three nuclear RNA polymerases and the absence of recognizable sequence motifs for DNA and nucleoside triphosphate-binding indicate that the common subunits do not have a catalytic role but are important for a function shared by the RNA polymerases such as transcriptional efficiency, nuclear localization, enzyme stability, or coordinate regulation of rRNA, mRNA, and tRNA synthesis. -
Targeting the RNA Polymerase I Transcription for Cancer Therapy Comes of Age
Targeting the RNA Polymerase I Transcription for Cancer Therapy Comes of Age Ferreira, R., Schneekloth, J. S., Panov, K. I., Hannan, K. M., & Hannan, R. D. (2020). Targeting the RNA Polymerase I Transcription for Cancer Therapy Comes of Age. Cells, 9(2). https://doi.org/10.3390/cells9020266 Published in: Cells Document Version: Publisher's PDF, also known as Version of record Queen's University Belfast - Research Portal: Link to publication record in Queen's University Belfast Research Portal Publisher rights © 2020 The Authors. This is an open access article published under a Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited. General rights Copyright for the publications made accessible via the Queen's University Belfast Research Portal is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights. Take down policy The Research Portal is Queen's institutional repository that provides access to Queen's research output. Every effort has been made to ensure that content in the Research Portal does not infringe any person's rights, or applicable UK laws. If you discover content in the Research Portal that you believe breaches copyright or violates any law, please contact [email protected]. Download date:26. Sep. 2021 cells Review Targeting the RNA Polymerase I Transcription for Cancer Therapy Comes of Age Rita Ferreira 1,* , John S.