Papers

Peer-reviewed
Mar, 2010

Multiple gamma-glutamylation: A novel type of post-translational modification in a diapausing Artemia cyst protein

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
  • Mai Hasegawa
  • ,
  • Yuka Ikeda
  • ,
  • Hideaki Kanzawa
  • ,
  • Mika Sakamoto
  • ,
  • Mina Goto
  • ,
  • Susumu Tsunasawa
  • ,
  • Toshio Uchiumi
  • ,
  • Shoji Odani

Volume
394
Number
1
First page
36
Last page
41
Language
English
Publishing type
Research paper (scientific journal)
DOI
10.1016/j.bbrc.2010.02.064
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE

A highly hydrophilic, glutamate-rich protein was identified in the aqueous phenol extract from the cytosolic fraction of brine shrimp (Artemia franciscana) diapausing cysts and termed Anemia phenol soluble protein (PSP). Mass spectrometric analysis revealed the presence of many protein peaks around m/z 11,000, separated by 129 atomic mass units; this value corresponds to that of glutamate, which is strongly suggestive of heterogeneous polyglutamylation. Polyglutamylation has long been known as the functionally important post-translational modification of tubulins, which carry poly(L-glutamic acid) chains of heterogeneous length branching off from the main chain at the gamma-carboxy groups of a few specific glutamate residues. In Artemia PSP, however, Edman degradation of enzymatic peptides revealed that at least 13, and presumably 16, glutamate residues were modified by the attachment of a single L-glutamate, representing a hitherto undescribed type of post-translational modification: namely, multiple gamma-glutamylation or the addition of a large number of glutamate residues along the polypeptide chain. Although biological significance of PSP and its modification is yet to be established, suppression of in vitro thermal aggregation of lactate dehydrogenase by glutamylated PSP was observed. (C) 2010 Elsevier Inc. All rights reserved.

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Link information
DOI
https://doi.org/10.1016/j.bbrc.2010.02.064
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/20170642
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000276474800007&DestApp=WOS_CPL
ID information
  • DOI : 10.1016/j.bbrc.2010.02.064
  • ISSN : 0006-291X
  • Pubmed ID : 20170642
  • Web of Science ID : WOS:000276474800007

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