Arginyltransferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms

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dc.contributor.authorHu, Rong-Gui
dc.contributor.authorBrower, Christopher S.
dc.contributor.authorWang, Haiqing
dc.contributor.authorDavydov, Ilia V.
dc.contributor.authorSheng, Jun
dc.contributor.authorZhou, Jianmin
dc.contributor.authorTae Kwon, Yong
dc.contributor.authorVarshavsky, Alexander
dc.creator.orcidhttps://orcid.org/0000-0003-0289-5541
dc.creator.orcidhttps://orcid.org/0000-0003-0289-5541
dc.date.accessioned2023-01-24T15:16:58Z
dc.date.available2023-01-24T15:16:58Z
dc.date.issued2006
dc.descriptionArticle originally published by Journal of Biological Chemistry, 281(43). English. Published online 2006. https://doi.org/10.1074/jbc.m604355200.
dc.description.abstractSubstrates of the N-end rule pathway include proteins with destabilizing N-terminal residues. Three of them, Asp, Glu, and (oxidized) Cys, function through their conjugation to Arg, one of destabilizing N-terminal residues that are recognized directly by the pathway’s ubiquitin ligases. The conjugation of Arg is mediated by arginyltransferase, encoded by ATE1. Through its regulated degradation of specific proteins, the arginylation branch of the N-end rule pathway mediates, in particular, the cardiovascular development, the fidelity of chromosome segregation, and the control of signaling by nitric oxide.We show that mouse ATE1 specifies at least six mRNA isoforms, which are produced through alternative splicing, encode enzymatically active arginyltransferases, and are expressed at varying levels in mouse tissues. We also show that the ATE1 promoter is bidirectional, mediating the expression of bothATE1 and an oppositely oriented, previously uncharacterized gene. In addition, we identified GRP78 (glucose-regulated protein 78) and protein-disulfide isomerase as putative physiological substrates of arginyltransferase. Purified isoforms of arginyltransferase that contain the alternative first exons differentially arginylate these proteins in extract from ATE1 / embryos, suggesting that specific isoforms may have distinct functions. Although the N-end rule pathway is apparently confined to the cytosol and the nucleus, and although GRP78 and protein-disulfide isomerase are located largely in the endoplasmic reticulum, recent evidence suggests that these proteins are also present in the cytosol and other compartments in vivo, where they may become N-end rule substrates.en_US
dc.identifier.citationThis is the published version of an article that is available at https://doi.org/10.1074/jbc.m604355200. Recommended citation: Hu, R.-G., Brower, C. S., Wang, H., Davydov, I. V., Sheng, J., Zhou, J., Kwon, Y. T., & Varshavsky, A. (2006). Arginyltransferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms. Journal of Biological Chemistry, 281(43), 32559–32573. This item has been deposited in accordance with publisher copyright and licensing terms and with the author’s permission.en_US
dc.identifier.urihttps://hdl.handle.net/11274/14338
dc.identifier.urihttps://doi.org/10.1074/jbc.m604355200
dc.language.isoen_USen_US
dc.publisherElsevieren_US
dc.rights.licenseCC-BY 4.0
dc.subjectUbiquitin ligasesen_US
dc.subjectUbiquitinen_US
dc.subjectPurified isoformsen_US
dc.titleArginyltransferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoformsen_US
dc.typeArticleen_US

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