Literature DB >> 22738983

Characterization of the C-terminal diglycine motif of SUMO-1/3.

Koji Yamada1, Miyuki Muramatsu, Daiki Saito, Mai Sato-Oka, Masayuki Saito, Taishi Moriyama, Hisato Saitoh.   

Abstract

A hallmark of small ubiquitin-related modifier (SUMO) is the production of a C-terminal tail containing diglycines (GGs), which are believed to be required for SUMOylation. Whether GGs are required components in SUMOylation remains unanswered experimentally. In this study we found that the SUMO-1/3-AA/-GS/-GN/-GA mutant can form sodium dodecyl sulfate (SDS)-dithiothreitol (DTT)-resistant complexes with cellular proteins, indicating that the GG motif is not strictly required for SUMOylation.

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Year:  2012        PMID: 22738983     DOI: 10.1271/bbb.120019

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  3 in total

1.  Small ubiquitin-like modifier (SUMO) isoforms and conjugation-independent function in DNA double-strand break repair pathways.

Authors:  Yiheng Hu; Jeffrey D Parvin
Journal:  J Biol Chem       Date:  2014-06-25       Impact factor: 5.157

2.  Mechanistic dissection of increased enzymatic rate in a phase-separated compartment.

Authors:  William Peeples; Michael K Rosen
Journal:  Nat Chem Biol       Date:  2021-05-25       Impact factor: 15.040

3.  Multiplexed Delivery of Synthetic (Un)Conjugatable Ubiquitin and SUMO2 Enables Simultaneous Monitoring of Their Localization and Function in Live Cells.

Authors:  Guy Mann; Pradeep Sadhu; Ashraf Brik
Journal:  Chembiochem       Date:  2022-03-11       Impact factor: 3.461

  3 in total

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