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Keywords: SUMO
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Articles

SUMO chain formation relies on the amino-terminal region of SUMO-conjugating enzyme and has dedicated substrates in plants

Konstantin Tomanov, Lilian Nehlin, Ionida Ziba, Andreas Bachmair
Journal: Biochemical Journal
Biochem J (2018) 475 (1): 61–74.
DOI: https://doi.org/10.1042/BCJ20170472
Published: 02 January 2018
...Konstantin Tomanov; Lilian Nehlin; Ionida Ziba; Andreas Bachmair The small ubiquitin-related modifier (SUMO) conjugation apparatus usually attaches single SUMO moieties to its substrates, but SUMO chains have also been identified. To better define the biochemical requirements and characteristics...
View article titled, <span class="search-highlight">SUMO</span> chain formation relies on the amino-terminal region of <span class="search-highlight">SUMO</span>-conjugating enzyme and has dedicated substrates in plants
Click here to open pdf in another window PDF for <span class="search-highlight">SUMO</span> chain formation relies on the amino-terminal region of <span class="search-highlight">SUMO</span>-conjugating enzyme and has dedicated substrates in plants
Includes: Supplementary data
Articles

E3 SUMO ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development

Sung-Il Kim, Bong Soo Park, Do Youn Kim, Song Yion Yeu, Sang Ik Song, Jong Tae Song, Hak Soo Seo
Journal: Biochemical Journal
Biochem J (2015) 469 (2): 299–314.
DOI: https://doi.org/10.1042/BJ20141302
Published: 06 July 2015
..., Cullin, F-box (SCF) SLY1 complex, are modulated at the post-translational level have not been addressed. In the present study, we show that the E3 SUMO (small ubiquitin-related modifier) ligase AtSIZ1 regulates gibberellic acid signalling in Arabidopsis species by sumoylating SLY1. SLY1 was less abundant...
View article titled, E3 <span class="search-highlight">SUMO</span> ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development
Click here to open pdf in another window PDF for E3 <span class="search-highlight">SUMO</span> ligase AtSIZ1 positively regulates SLY1-mediated GA signalling and plant development
Includes: Supplementary data
Articles

Ubiquitin C-terminal hydrolases cleave isopeptide- and peptide-linked ubiquitin from structured proteins but do not edit ubiquitin homopolymers

John S. Bett, Maria Stella Ritorto, Richard Ewan, Ellis G. Jaffray, Satpal Virdee, Jason W. Chin, Axel Knebel, Thimo Kurz, Matthias Trost, Michael H. Tatham, Ronald T. Hay
Journal: Biochemical Journal
Biochem J (2015) 466 (3): 489–498.
DOI: https://doi.org/10.1042/BJ20141349
Published: 06 March 2015
... and neurodegeneration but whose substrate preference has remained unclear. In addition, our findings suggest that the reversal of Ube2W-mediated N-terminal ubiquitylation may be one physiological role of UCH DUBs in vivo . BAP1 SUMO Ube2W ubiquitin UCH-L1 UCH-L3 UCH-L5 The substrate preference...
View article titled, Ubiquitin C-terminal hydrolases cleave isopeptide- and peptide-linked ubiquitin from structured proteins but do not edit ubiquitin homopolymers
Click here to open pdf in another window PDF for Ubiquitin C-terminal hydrolases cleave isopeptide- and peptide-linked ubiquitin from structured proteins but do not edit ubiquitin homopolymers
Includes: Supplementary data
Articles

Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family

Marcin Drag, Jowita Mikolajczyk, I. M. Krishnakumar, Ziwei Huang, Guy S. Salvesen
Journal: Biochemical Journal
Biochem J (2008) 409 (2): 461–469.
DOI: https://doi.org/10.1042/BJ20070940
Published: 21 December 2007
...Marcin Drag; Jowita Mikolajczyk; I. M. Krishnakumar; Ziwei Huang; Guy S. Salvesen SENPs [Sentrin/SUMO (small ubiquitin-related modifier)-specific proteases] include proteases that activate the precursors of SUMOs, or deconjugate SUMOs attached to target proteins. SENPs are usually assayed...
View article titled, Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family
Click here to open pdf in another window PDF for Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family
Includes: Supplementary data