Please use this identifier to cite or link to this item: http://223.31.159.10:8080/jspui/handle/123456789/1129
Full metadata record
DC FieldValueLanguage
dc.contributor.authorKamble, Nitin Uttam-
dc.contributor.authorMajee, Manoj-
dc.date.accessioned2020-12-01T09:50:00Z-
dc.date.available2020-12-01T09:50:00Z-
dc.date.issued2020-
dc.identifier.citationBiochemical Journal, 477(22): 4453-4471en_US
dc.identifier.issn1470-8728-
dc.identifier.otherhttps://doi.org/10.1042/BCJ20200794-
dc.identifier.urihttps://portlandpress.com/biochemj/article-abstract/477/22/4453/227075/PROTEIN-l-ISOASPARTYL-METHYLTRANSFERASE-PIMT-in?redirectedFrom=fulltext-
dc.identifier.urihttp://223.31.159.10:8080/jspui/handle/123456789/1129-
dc.descriptionAccepted date: November 10 2020en_US
dc.description.abstractProteins are essential molecules that carry out key functions in a cell. However, as a result of aging or stressful environments, the protein undergoes a range of spontaneous covalent modifications, including the formation of abnormal l-isoaspartyl residues from aspartyl or asparaginyl residues, which can disrupt the protein's inherent structure and function. PROTEIN l-ISOASPARTYL METHYLTRANSFERASE (PIMT: EC 2.1.1.77), an evolutionarily conserved ancient protein repairing enzyme (PRE), converts such abnormal l-isoaspartyl residues to normal l-aspartyl residues and re-establishes the protein's native structure and function. Although originally discovered in animals as a PRE, PIMT emerged as a key PRE in plants, particularly in seeds, in which PIMT plays a predominant role in preserving seed vigor and viability for prolonged periods of time. Interestingly, higher plants encode a second PIMT (PIMT2) protein which possesses a unique N-terminal extension, and exhibits several distinct features and far more complexity than non-plant PIMTs. Recent studies indicate that the role of PIMT is not restricted to preserving seed vigor and longevity but is also implicated in enhancing the growth and survivability of plants under stressful environments. Furthermore, expression studies indicate the tantalizing possibility that PIMT is involved in various physiological processes apart from its role in seed vigor, longevity and plant's survivability under abiotic stress. This review article particularly describes new insights and emerging interest in all facets of this enzyme in plants along with a concise comparative overview on isoAsp formation, and the role and regulation of PIMTs across evolutionary diverse species. Additionally, recent methods and their challenges in identifying isoaspartyl containing proteins (PIMT substrates) are highlighted.en_US
dc.language.isoen_USen_US
dc.publisherPortland Pressen_US
dc.subjectabiotic stressen_US
dc.subjectisoaspartylen_US
dc.subjectprotein damageen_US
dc.subjectprotein l-isoaspartyl methyltransferaseen_US
dc.subjectprotein repairen_US
dc.subjectseeden_US
dc.titlePROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT) in plants: regulations and functionsen_US
dc.typeArticleen_US
Appears in Collections:Institutional Publications

Files in This Item:
File Description SizeFormat 
Majee M_2020_5.pdf
  Restricted Access
2.57 MBAdobe PDFView/Open Request a copy


Items in IR@NIPGR are protected by copyright, with all rights reserved, unless otherwise indicated.