MRPS7 Rabbit Pab

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Leader in Biomolecular Solutions for Life Science MRPS7 Rabbit pAb Catalog No.: A16272 Basic Information Background Catalog No. Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in A16272 protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% Observed MW protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is 28kDa reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins Calculated MW comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical 28kDa properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein. In the prokaryotic ribosome, the comparable protein is thought to Category play an essential role in organizing the 3' domain of the 16 S rRNA in the vicinity of the P- and A-sites. Pseudogenes corresponding to this gene are found on chromosomes 8p Primary antibody and 12p. Applications WB Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 51081 Q9Y2R9 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 110-190 of human MRPS7 (NP_057055.2). Synonyms MRPS7;MRP-S;MRP-S7;RP-S7;RPMS7;S7mt;bMRP27a Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using MRPS7 antibody (A16272) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (RM00020). Exposure time: 90s. Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

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1 AGING Supplementary Table 2
SUPPLEMENTARY TABLES Supplementary Table 1. Details of the eight domain chains of KIAA0101. Serial IDENTITY MAX IN COMP- INTERFACE ID POSITION RESOLUTION EXPERIMENT TYPE number START STOP SCORE IDENTITY LEX WITH CAVITY A 4D2G_D 52 - 69 52 69 100 100 2.65 Å PCNA X-RAY DIFFRACTION √ B 4D2G_E 52 - 69 52 69 100 100 2.65 Å PCNA X-RAY DIFFRACTION √ C 6EHT_D 52 - 71 52 71 100 100 3.2Å PCNA X-RAY DIFFRACTION √ D 6EHT_E 52 - 71 52 71 100 100 3.2Å PCNA X-RAY DIFFRACTION √ E 6GWS_D 41-72 41 72 100 100 3.2Å PCNA X-RAY DIFFRACTION √ F 6GWS_E 41-72 41 72 100 100 2.9Å PCNA X-RAY DIFFRACTION √ G 6GWS_F 41-72 41 72 100 100 2.9Å PCNA X-RAY DIFFRACTION √ H 6IIW_B 2-11 2 11 100 100 1.699Å UHRF1 X-RAY DIFFRACTION √ www.aging-us.com 1 AGING Supplementary Table 2. Significantly enriched gene ontology (GO) annotations (cellular components) of KIAA0101 in lung adenocarcinoma (LinkedOmics). Leading Description FDR Leading Edge Gene EdgeNum RAD51, SPC25, CCNB1, BIRC5, NCAPG, ZWINT, MAD2L1, SKA3, NUF2, BUB1B, CENPA, SKA1, AURKB, NEK2, CENPW, HJURP, NDC80, CDCA5, NCAPH, BUB1, ZWILCH, CENPK, KIF2C, AURKA, CENPN, TOP2A, CENPM, PLK1, ERCC6L, CDT1, CHEK1, SPAG5, CENPH, condensed 66 0 SPC24, NUP37, BLM, CENPE, BUB3, CDK2, FANCD2, CENPO, CENPF, BRCA1, DSN1, chromosome MKI67, NCAPG2, H2AFX, HMGB2, SUV39H1, CBX3, TUBG1, KNTC1, PPP1CC, SMC2, BANF1, NCAPD2, SKA2, NUP107, BRCA2, NUP85, ITGB3BP, SYCE2, TOPBP1, DMC1, SMC4, INCENP. RAD51, OIP5, CDK1, SPC25, CCNB1, BIRC5, NCAPG, ZWINT, MAD2L1, SKA3, NUF2, BUB1B, CENPA, SKA1, AURKB, NEK2, ESCO2, CENPW, HJURP, TTK, NDC80, CDCA5, BUB1, ZWILCH, CENPK, KIF2C, AURKA, DSCC1, CENPN, CDCA8, CENPM, PLK1, MCM6, ERCC6L, CDT1, HELLS, CHEK1, SPAG5, CENPH, PCNA, SPC24, CENPI, NUP37, FEN1, chromosomal 94 0 CENPL, BLM, KIF18A, CENPE, MCM4, BUB3, SUV39H2, MCM2, CDK2, PIF1, DNA2, region CENPO, CENPF, CHEK2, DSN1, H2AFX, MCM7, SUV39H1, MTBP, CBX3, RECQL4, KNTC1, PPP1CC, CENPP, CENPQ, PTGES3, NCAPD2, DYNLL1, SKA2, HAT1, NUP107, MCM5, MCM3, MSH2, BRCA2, NUP85, SSB, ITGB3BP, DMC1, INCENP, THOC3, XPO1, APEX1, XRCC5, KIF22, DCLRE1A, SEH1L, XRCC3, NSMCE2, RAD21.
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A Homozygous MRPL24 Mutation Causes a Complex Movement Disorder and Affects the Mitoribosome Assembly T
Neurobiology of Disease 141 (2020) 104880 Contents lists available at ScienceDirect Neurobiology of Disease journal homepage: www.elsevier.com/locate/ynbdi A homozygous MRPL24 mutation causes a complex movement disorder and affects the mitoribosome assembly T Michela Di Nottiaa,1, Maria Marcheseb,1, Daniela Verrignia, Christian Daniel Muttic, Alessandra Torracoa, Romina Olivad, Erika Fernandez-Vizarrac, Federica Moranib, Giulia Trania, Teresa Rizzaa, Daniele Ghezzie,f, Anna Ardissoneg,h, Claudia Nestib, Gessica Vascoi, Massimo Zevianic, Michal Minczukc, Enrico Bertinia, Filippo Maria Santorellib,2, ⁎ Rosalba Carrozzoa, ,2 a Unit of Muscular and Neurodegenerative Disorders, Laboratory of Molecular Medicine, Bambino Gesù Children's Hospital, IRCCS, Rome, Italy b Molecular Medicine & Neurogenetics, IRCCS Fondazione Stella Maris, Pisa, Italy c MRC Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK d Department of Sciences and Technologies, University Parthenope of Naples, Naples, Italy e Unit of Medical Genetics and Neurogenetics, Fondazione IRCCS Istituto Neurologico Carlo Besta, Milan, Italy f Department of Pathophysiology and Transplantation, University of Milan, Milan, Italy g Child Neurology Unit, Fondazione IRCCS Istituto Neurologico Carlo Besta, Milan, Italy h Department of Molecular and Translational Medicine DIMET, University of Milan-Bicocca, Milan, Italy i Department of Neurosciences, IRCCS Bambino Gesù Children Hospital, Rome, Italy ARTICLE INFO ABSTRACT Keywords: Mitochondrial ribosomal protein large 24 (MRPL24) is 1 of the 82 protein components of mitochondrial ribo- Mitochondrial disorders somes, playing an essential role in the mitochondrial translation process. Movement disorder We report here on a baby girl with cerebellar atrophy, choreoathetosis of limbs and face, intellectual dis- MRPL24 ability and a combined defect of complexes I and IV in muscle biopsy, caused by a homozygous missense mu- Mitoribosomes tation identified in MRPL24.
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The Pennsylvania State University the Graduate School Eberly
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CLPP Coordinates Mitoribosomal Assembly Through the Regulation of ERAL1 Levels
Article CLPP coordinates mitoribosomal assembly through the regulation of ERAL1 levels Karolina Szczepanowska1,2,†, Priyanka Maiti1,2,†, Alexandra Kukat1,2, Eduard Hofsetz1,2, Hendrik Nolte1,3, Katharina Senft1,2, Christina Becker1,2, Benedetta Ruzzenente4, Hue-Tran Hornig-Do1,5, Rolf Wibom6, Rudolf J Wiesner1,5, Marcus Krüger1,3 & Aleksandra Trifunovic1,2,* Abstract the elimination of specific proteins when they are no longer needed. The irreversible nature of this process demands rigorous selectivity Despite being one of the most studied proteases in bacteria, very in the choice of substrates and the degradation timing. In prokary- little is known about the role of ClpXP in mitochondria. We now otes, regulated protein degradation is governed by energy-dependent present evidence that mammalian CLPP has an essential role in proteases, of which ClpXP is probably the best studied as it contri- determining the rate of mitochondrial protein synthesis by regu- butes to a large fraction of protein turnover in bacteria (Sauer & lating the level of mitoribosome assembly. Through a proteomic Baker, 2011). ClpXP is a highly conserved proteasome-like machin- approach and the use of a catalytically inactive CLPP, we produced ery present in all bacterial species and is also found in the mitochon- the first comprehensive list of possible mammalian ClpXP dria and chloroplasts of eukaryotic cells (Sauer & Baker, 2011). In substrates involved in the regulation of mitochondrial translation, mammals, ClpXP protein substrates are recognized and unfolded by oxidative phosphorylation, and a number of metabolic pathways. the hexameric AAA+ protein CLPX that delivers them to the CLPP We further show that the defect in mitoribosomal assembly is a protease for degradation (Sauer & Baker, 2011).
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Transcriptomic and Proteomic Landscape of Mitochondrial
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Additional Tables.Xlsx
Additional Table 5 Enriched pathways of upregulated DEGs after spinal cord injury in WT (P < 0.05, q < 0.05) Database Description Ratio of DEGs Ratio of P -value P adjust q value gene name GO ribosomal subunit 87/755 214/12262 1.03E-49 4.61E-47 4.20E-47 Gm6576/Gm10036/Gm5786/Mrps28/Gm9493/Rpl13- ps3/Rpl7l1/Mrpl10/Mrpl44/Rps20/Mrpl51/Mrps11/Mpv17l2/Mrps7/Gm10020/Gm10073 /Mrpl2/Mrpl52/Rpl22/Mrpl4/Mrps24/Zcchc17/Rpl28/Mrpl34/Rpl29/Mrps36/Rpl9- ps6/Hba-a2/Hba-a1/Rpl23a- ps3/Rpl15/Rack1/Mrps18a/Mrpl28/Rpl10a/Mrpl12/Rpl18/Rpl35a/Mrpl41/Mrps12/Rpl36 a/Rps9/Rps18/Rps5/Rps27a/Rps24/Rplp2/Rpl14/Mrpl30/Rps6/Rpl6/Rps3/Rps4x/Rpsa/R pl7/Rpl27a/Rps23/Rps10/Mrps21/Rpl36/Rpl30/Rps17/Mrpl42/Rpl35/Rpl27/Rplp0/Rps28 /Rpl31/Rpl39/Rps13/Rpl13/Rps11/Rpl8/Rps3a1/Fau/Rpl9/Rpl3/Rpl26/Rps15/Rpl13a/Uba 52/Rpl24/Rpl19/Rps14/Rpl4/Rps27/Rplp1 GO ribosome 93/755 248/12262 1.67E-49 4.61E-47 4.20E-47 Gm6576/Pnpt1/Gm10036/Gm5786/Mrps28/Gm9493/Rpl13- ps3/Rpl7l1/Mrpl10/Mrpl44/Rps20/Mrpl51/Mrps11/Mpv17l2/Mrps7/Gm10020/Gm10073 /Mrpl2/Mrpl52/Rpl22/Mrpl4/Mrps24/Zcchc17/Rpl28/Mrpl34/Rpl29/Mrps36/Rpl9- ps6/Hba-a2/Hba-a1/Rpl23a- ps3/Rpl15/Rack1/Eif3h/Mrps18a/Mrpl28/Mrps33/Rpl10a/Mrpl12/Rpl18/Rpl35a/Btf3/Mrp l41/Mrps12/Rpl36a/Rps9/Rps18/Rps5/Rps27a/Rps24/Rplp2/Rpl14/Mrpl30/Rps6/Rpl6/R ps3/Rps4x/Rpsa/Rpl7/Rpl27a/Rps23/Rps10/Mrps21/Rpl36/Rpl30/Rps17/Mrpl42/Rpl35/R pl27/Rplp0/Rps28/Rpl31/Rpl39/Rps13/Rpl13/Rps11/Rpl8/Rps3a1/Fau/Rpl9/Rpl3/Rpl26/ Rps15/Rpl13a/Uba52/Rpl41/Rpl24/Rpl19/Rps14/Rpl4/Ndufa7/Rps27/Rplp1 GO structural constituent of 76/733 169/11958 1.65E-47 1.16E-44 1.12E-44 Gm6576/Gm10036/Gm5786/Rpl7l1/Mrpl10/Rps20/Mrpl51/Mrps11/Mrps7/Gm10020/G
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Impaired Mitochondrial Biogenesis in Adipose Tissue in Acquired Obesity
Diabetes Volume 64, September 2015 3135 Sini Heinonen,1 Jana Buzkova,2 Maheswary Muniandy,1 Risto Kaksonen,1,3 Miina Ollikainen,4 Khadeeja Ismail,4 Antti Hakkarainen,5 Jesse Lundbom,5,6 Nina Lundbom,5 Katriina Vuolteenaho,7 Eeva Moilanen,7 Jaakko Kaprio,8,9,10 Aila Rissanen,1,11 Anu Suomalainen,2,12 and Kirsi H. Pietiläinen1,8,13 Impaired Mitochondrial Biogenesis in Adipose Tissue in Acquired Obesity Diabetes 2015;64:3135–3145 | DOI: 10.2337/db14-1937 Low mitochondrial number and activity have been sug- and OXPHOS proteins in SAT are downregulated in ac- gested as underlying factors in obesity, type 2 diabetes, quired obesity, and are associated with metabolic distur- and metabolic syndrome. However, the stage at which bances already at the preclinical stage. mitochondrial dysfunction manifests in adipose tissue after the onset of obesity remains unknown. Here we examined subcutaneous adipose tissue (SAT) samples Adipocytes are important contributors to energy balance – from healthy monozygotic twin pairs, 22.8 36.2 years of and metabolic homeostasis. Within these highly dynamic D > 2 age, who were discordant ( BMI 3kg/m, mean length cells, mitochondria are at the center of energy metabo- OBESITY STUDIES 6 n of discordance 6.3 0.3 years, = 26) and concordant lism, using carbohydrates, lipids, and proteins to produce D < 2 n ( BMI 3kg/m, = 14) for body weight, and assessed ATP and metabolites for growth, as well as contributing to their detailed mitochondrial metabolic characteristics: adipocyte differentiation and maturation (1). Mitochon- mitochondrial-related transcriptomes with dysregulated dria possess their own multicopy genome, a 16.6-kb cir- pathways, mitochondrial DNA (mtDNA) amount, mtDNA- cular mitochondrial DNA (mtDNA) that encodes two encoded transcripts, and mitochondrial oxidative phos- phorylation (OXPHOS) protein levels.
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Predicting Glioblastoma Prognosis Networks Using Weighted Gene Co-Expression Network Analysis on TCGA Data
Faculty & Staff Scholarship 2012 Predicting glioblastoma prognosis networks using weighted gene co-expression network analysis on TCGA data Yang Xiang Cun-Quan Zhang Kun Huang Follow this and additional works at: https://researchrepository.wvu.edu/faculty_publications Xiang et al. BMC Bioinformatics 2012, 13(Suppl 2):S12 http://www.biomedcentral.com/1471-2105/13/S2/S12 PROCEEDINGS Open Access Predicting glioblastoma prognosis networks using weighted gene co-expression network analysis on TCGA data Yang Xiang1, Cun-Quan Zhang2, Kun Huang1,3* From Great Lakes Bioinformatics Conference 2011 Athens, OH, USA. 2-4 May 2011 Abstract Background: Using gene co-expression analysis, researchers were able to predict clusters of genes with consistent functions that are relevant to cancer development and prognosis. We applied a weighted gene co-expression network (WGCN) analysis algorithm on glioblastoma multiforme (GBM) data obtained from the TCGA project and predicted a set of gene co-expression networks which are related to GBM prognosis. Methods: We modified the Quasi-Clique Merger algorithm (QCM algorithm) into edge-covering Quasi-Clique Merger algorithm (eQCM) for mining weighted sub-network in WGCN. Each sub-network is considered a set of features to separate patients into two groups using K-means algorithm. Survival times of the two groups are compared using log-rank test and Kaplan-Meier curves. Simulations using random sets of genes are carried out to determine the thresholds for log-rank test p-values for network selection. Sub-networks with p-values less than their corresponding thresholds were further merged into clusters based on overlap ratios (>50%). The functions for each cluster are analyzed using gene ontology enrichment analysis.
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Comprehensive Mitochondrial Nuclear Gene Panel
Comprehensive Mitochondrial Nuclear Gene Panel Test Code D4606 Test Summary This panel analyzes 254 genes that have been associated with mitochondrial disorders in nuclear genes. Turn-Around-Time (TAT)* 3 - 5 weeks Acceptable Sample Types Whole Blood (EDTA) (Preferred sample type) DNA, Isolated Dried Blood Spots Saliva Acceptable Billing Types Self (patient) Payment Institutional Billing Commercial Insurance Indications for Testing This test may be appropriate for individuals who have a clinical suspicion of a mitochondrial disorder and/or family history of a mitochondrial disorder. Test Description This panel analyzes 254 genes that have been associated with mitochondrial disorders in nuclear genes. Both sequencing and deletion/duplication (CNV) analysis will be performed on the coding regions of all genes included (unless otherwise marked). All analysis is performed utilizing Next Generation Sequencing (NGS) technology. CNV analysis is designed to detect deletions and duplications of three exons or greater in size. All variants are classified according to ACMG guidelines. Condition Description Mitochondrial disease is a varied group of disorders characterized by impaired energy production. Hallmarks of mitochondrial disease include neurological, cardiovascular, ophthalmologic and gastroenterological features. It is estimated that 1/5,000 individuals has a genetic mitochondrial disease. Genes AARS, AARS2, ABCB11, ABCB4, ABCB7, ABCD4, ACAD9, ACADM, ACADVL, ACO2, ACSF3, ADCK3, ADCK4, AFG3L2, AGK, AGL, AIFM1, ALAS2, ALDOA, ALDOB, ALG1,
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Mitochondrial Ribosomal Proteins: Candidate Genes for Mitochondrial Disease James E
March/April 2004 ⅐ Vol. 6 ⅐ No. 2 review Mitochondrial ribosomal proteins: Candidate genes for mitochondrial disease James E. Sylvester, PhD1, Nathan Fischel-Ghodsian, MD2, Edward B. Mougey, PhD1, and Thomas W. O’Brien, PhD3 Most of the energy requirement for cell growth, differentiation, and development is met by the mitochondria in the form of ATP produced by the process of oxidative phosphorylation. Human mitochondrial DNA encodes a total of 13 proteins, all of which are essential for oxidative phosphorylation. The mRNAs for these proteins are translated on mitochondrial ribosomes. Recently, the genes for human mitochondrial ribosomal proteins (MRPs) have been identified. In this review, we summarize their refined chromosomal location. It is well known that mutations in the mitochondrial translation system, i.e., ribosomal RNA and transfer RNA cause various pathologies. In this review, we suggest possible associations between clinical conditions and MRPs based on coincidence of genetic map data and chromosomal location. These MRPs may be candidate genes for the clinical condition or may act as modifiers of existing known gene mutations (mt-tRNA, mt-rRNA, etc.). Genet Med 2004:6(2):73–80. Key Words: mitochondrial, ribosomal proteins, oxidative phosphorylation, candidate genes, translation Most of the energy requirements for cell growth, differenti- THE MITORIBOSOME ation, and development are met by the mitochondrial ATP Human cells contain two genomes and two protein synthe- produced by the process of oxidative phosphorylation. Mito- sizing (translation) systems. The first is the nuclear genome of chondrial DNA encodes 13 essential proteins of this oxidative 3 ϫ 109 bp that has 30,000 to 40,000 genes coding a much phosphorylation system.
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