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ATP5G3  -  ATP synthase, H+ transporting,...

Homo sapiens

Synonyms: ATP synthase F(0) complex subunit C3, mitochondrial, ATP synthase lipid-binding protein, ATP synthase proteolipid P3, ATP synthase proton-transporting mitochondrial F(0) complex subunit C3, ATPase protein 9, ...
 
 
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Disease relevance of ATP5G3

  • We have studied the allele specific expression of c-myc P0- and P3-RNA in Burkitt's lymphoma (BL) cells [1].
  • By phenotypic and molecular genetic criteria, this double mutant (H104A-HS9) was shown to be able to undergo significant RNA splicing, thus confirming the existence and functional importance of the long-range P3 pairing region in this phage intron [2].
  • RNAs encoding wild-type forms of protein 3AB or the P3 precursor polypeptide were cotranslated with full-length poliovirus RNAs containing the F69H mutation in a HeLa cell-free translation/replication assay in an attempt to trans complement the RNA replication defect exhibited by the 3AB(F69H) lesion [3].
  • The viral shell has been investigated using time and temperature resolved Raman and ultraviolet-resonance Raman spectroscopy to reveal novel features of the capsid structure and its pathway of assembly from P3 subunits [4].
  • One dicistronic genome was constructed in which the poliovirus 5' nontranslated region was fused to the gene encoding luciferase, followed by the complete EMCV IRES fused to the P2-P3 region of the poliovirus genome (PV-Luc-EMCV) [5].
 

Psychiatry related information on ATP5G3

 

High impact information on ATP5G3

  • Studies with synthetic peptide analogs indicated that both forms of NRk had similar specificity determinants, requiring a basic residue at P-3 (i.e., three amino acids N-terminal to the phosphorylated serine) and a hydrophobic residue at P-5 [9].
  • MRK preferentially phosphorylates R-P-X-S/T-P sites, with the preference for arginine at position -3 (P-3) being more stringent than for prolines at P-2 and P+1 [10].
  • The inhibition of P3 luciferase expression by p53 was more pronounced in the two cell lines that expressed mutant p53 protein, RD, and HTB114 [11].
  • Regulation of insulin-like growth factor II P3 promotor by p53: a potential mechanism for tumorigenesis [11].
  • The observation that the mitochondrial ATPase subunit c protein accumulates in this disease suggests that autophagy, a pathway that regulates mitochondrial turnover, may be disrupted [12].
 

Biological context of ATP5G3

 

Anatomical context of ATP5G3

 

Associations of ATP5G3 with chemical compounds

  • Guanidine hydrochloride (GuHCl) dissociation of the P3 shell yields similar results [4].
  • These inhibitors, which are of the hydroxyethylene and statine types, respectively, possess a cyclohexylalanine side chain at P1 and have interesting functionalities at the P3 position which, until now, have not been subjected to crystallographic analysis [20].
  • Time course studies of mRNA accumulation of two of them (P3- and P4-chitinases) have been studied upon virus infection, mercuric chloride treatment and UV irradiation [21].
  • Mab Mano 4/4 is directed against a 28 kD glycoprotein and mab 486 P 3/12 is reacting with a 200 kD glycoprotein belonging to the family of CEA-like proteins [18].
  • In reconstitution assays, proteins P1, P2, P4 and the previously reported lipoamide dehydrogenase (P3) had to be present to achieve glycine decarboxylase or synthase activity [22].
 

Other interactions of ATP5G3

  • In a trial screen using 28 shRNA vectors, another known gene, CDKN1A, and one new radiation susceptibility gene, ATP5G3, were identified [23].
 

Analytical, diagnostic and therapeutic context of ATP5G3

  • Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3) [14].
  • Synthetic peptide duplicating the 365-383 sequence in gamma C, designated P3, efficiently inhibited clot retraction in a dose-dependent manner [24].
  • HIV-positive patients had longer latency and reduced amplitude of the P300 (P3) component of the AEP compared with a normal control group, but were electrophysiologically similar to a matched control group of HIV-seronegative drug users [25].
  • Characterization by analytical ultracentrifugation indicates that below 8 mg/ml, the purified shell disassembles primarily into P3 trimers; at higher concentrations, larger multimers of P3 are formed [4].
  • Northern blots showed either slightly reduced hybridization of the 10.5-kb AR transcript (P3) or no hybridization (P1, P2), as confirmed by semiquantitative RT-PCR [26].

References

  1. Expression of P0- and P3-RNA from the normal and translocated c-myc allele in Burkitt's lymphoma cells. Eick, D., Polack, A., Kofler, E., Lenoir, G.M., Rickinson, A.B., Bornkamm, G.W. Oncogene (1990) [Pubmed]
  2. A non-directed, hydroxylamine-generated suppressor mutation in the P3 pairing region of the bacteriophage T4 td intron partially restores self-splicing capability. Brown, M.D., DeYoung, K.L., Hall, D.H. Mol. Microbiol. (1994) [Pubmed]
  3. Rescue of defective poliovirus RNA replication by 3AB-containing precursor polyproteins. Towner, J.S., Mazanet, M.M., Semler, B.L. J. Virol. (1998) [Pubmed]
  4. Structure, interactions and dynamics of PRD1 virus I. Coupling of subunit folding and capsid assembly. Tuma, R., Bamford, J.H., Bamford, D.H., Russell, M.P., Thomas, G.J. J. Mol. Biol. (1996) [Pubmed]
  5. Inherent instability of poliovirus genomes containing two internal ribosome entry site (IRES) elements supports a role for the IRES in encapsidation. Johansen, L.K., Morrow, C.D. J. Virol. (2000) [Pubmed]
  6. Auditory P300 in borderline personality disorder and schizophrenia. Kutcher, S.P., Blackwood, D.H., St Clair, D., Gaskell, D.F., Muir, W.J. Arch. Gen. Psychiatry (1987) [Pubmed]
  7. P3 and other long latency auditory evoked potentials in presenile dementia Alzheimer type and alcoholic Korsakoff syndrome. St Clair, D.M., Blackwood, D.H., Christie, J.E. The British journal of psychiatry : the journal of mental science. (1985) [Pubmed]
  8. Policosanol, reaction time and event-related potentials. Fontani, G., Maffei, D., Lodi, L. Neuropsychobiology (2000) [Pubmed]
  9. Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. Bachmann, M., Shiraishi, N., Campbell, W.H., Yoo, B.C., Harmon, A.C., Huber, S.C. Plant Cell (1996) [Pubmed]
  10. Identification of Yin-Yang Regulators and a Phosphorylation Consensus for Male Germ Cell-Associated Kinase (MAK)-Related Kinase. Fu, Z., Larson, K.A., Chitta, R.K., Parker, S.A., Turk, B.E., Lawrence, M.W., Kaldis, P., Galaktionov, K., Cohn, S.M., Shabanowitz, J., Hunt, D.F., Sturgill, T.W. Mol. Cell. Biol. (2006) [Pubmed]
  11. Regulation of insulin-like growth factor II P3 promotor by p53: a potential mechanism for tumorigenesis. Zhang, L., Kashanchi, F., Zhan, Q., Zhan, S., Brady, J.N., Fornace, A.J., Seth, P., Helman, L.J. Cancer Res. (1996) [Pubmed]
  12. Autophagy is disrupted in a knock-in mouse model of juvenile neuronal ceroid lipofuscinosis. Cao, Y., Espinola, J.A., Fossale, E., Massey, A.C., Cuervo, A.M., MacDonald, M.E., Cotman, S.L. J. Biol. Chem. (2006) [Pubmed]
  13. Rat mitochondrial ATP synthase ATP5G3: cloning and upregulation in pancreas after chronic ethanol feeding. Li, H.S., Zhang, J.Y., Thompson, B.S., Deng, X.Y., Ford, M.E., Wood, P.G., Stolz, D.B., Eagon, P.K., Whitcomb, D.C. Physiol. Genomics (2001) [Pubmed]
  14. Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3). Yan, W.L., Lerner, T.J., Haines, J.L., Gusella, J.F. Genomics (1994) [Pubmed]
  15. Identification of two distinct isoforms of stathmin and characterization of their respective phosphorylated forms. Beretta, L., Houdouin, F., Sobel, A. J. Biol. Chem. (1989) [Pubmed]
  16. Characterization of myelin fractions from human brain white matter. Cruz, T.F., Moscarello, M.A. J. Neurochem. (1985) [Pubmed]
  17. Translation of hepatitis A virus RNA in vitro: aberrant internal initiations influenced by 5' noncoding region. Jia, X.Y., Scheper, G., Brown, D., Updike, W., Harmon, S., Richards, O., Summers, D., Ehrenfeld, E. Virology (1991) [Pubmed]
  18. Monoclonal antibodies for characterization of the heterogeneity of normal and malignant transitional cells. Arndt, R., Dürkopf, H., Huland, H., Donn, F., Loening, T., Kalthoff, H. J. Urol. (1987) [Pubmed]
  19. CLC-3 deficiency leads to phenotypes similar to human neuronal ceroid lipofuscinosis. Yoshikawa, M., Uchida, S., Ezaki, J., Rai, T., Hayama, A., Kobayashi, K., Kida, Y., Noda, M., Koike, M., Uchiyama, Y., Marumo, F., Kominami, E., Sasaki, S. Genes Cells (2002) [Pubmed]
  20. X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors. Cooper, J., Quail, W., Frazao, C., Foundling, S.I., Blundell, T.L., Humblet, C., Lunney, E.A., Lowther, W.T., Dunn, B.M. Biochemistry (1992) [Pubmed]
  21. Differential expression of bean chitinase genes by virus infection, chemical treatment and UV irradiation. Margis-Pinheiro, M., Martin, C., Didierjean, L., Burkard, G. Plant Mol. Biol. (1993) [Pubmed]
  22. Purification and partial characterization of the glycine decarboxylase multienzyme complex from Eubacterium acidaminophilum. Freudenberg, W., Andreesen, J.R. J. Bacteriol. (1989) [Pubmed]
  23. A fast, simple method for screening radiation susceptibility genes by RNA interference. Tsuji, A.B., Sudo, H., Sugyo, A., Otsuki, M., Miyagishi, M., Taira, K., Imai, T., Harada, Y.N. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  24. Identification of a novel binding site for platelet integrins alpha IIb beta 3 (GPIIbIIIa) and alpha 5 beta 1 in the gamma C-domain of fibrinogen. Podolnikova, N.P., Yakubenko, V.P., Volkov, G.L., Plow, E.F., Ugarova, T.P. J. Biol. Chem. (2003) [Pubmed]
  25. The Edinburgh cohort of HIV-positive drug users: auditory event-related potentials show progressive slowing in patients with Centers for Disease Control stage IV disease. Goodwin, G.M., Chiswick, A., Egan, V., St Clair, D., Brettle, R.P. AIDS (1990) [Pubmed]
  26. Molecular features and clinical phenotypes in androgen insensitivity syndrome in the absence and presence of androgen receptor gene mutations. Holterhus, P.M., Werner, R., Hoppe, U., Bassler, J., Korsch, E., Ranke, M.B., Dörr, H.G., Hiort, O. J. Mol. Med. (2005) [Pubmed]
 
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