SUMO Chain Formation by Plant Enzymes

Tomanov, Konstantin; Ziba, Ionida; Bachmair, Andreas

doi:10.1007/978-1-4939-3759-2_8

Cited by 4 publications

(3 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Proteins for in vitro enzyme reactions were expressed and purified as described [ 11 , 18 ]. For isothermal titration calorimetry (ITC), SCE was further purified using a MonoS (GE Healthcare) ion exchange column on an ÄKTA 900 FPLC machine (GE Healthcare).…”

Section: Methodsmentioning

confidence: 99%

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

Tomanov

Nehlin

Ziba

et al. 2018

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

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 of SUMO chain formation, mutations in surface-exposed Lys residues of Arabidopsis SUMO-conjugating enzyme (SCE) were tested for in vitro activity. Lys-to-Arg changes in the amino-terminal region of SCE allowed SUMO acceptance from SUMO-activating enzyme and supported substrate mono-sumoylation, but these mutations had significant effects on SUMO chain assembly. We found no indication that SUMO modification of SCE promotes chain formation. A substrate was identified that is modified by SUMO chain addition, showing that SCE can distinguish substrates for either mono-sumoylation or SUMO chain attachment. It is also shown that SCE with active site Cys mutated to Ser can accept SUMO to form an oxyester, but cannot transfer this SUMO moiety onto substrates, explaining a previously known dominant negative effect of this mutation.

show abstract

Section: Methodsmentioning

confidence: 99%

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

Tomanov

Nehlin

Ziba

et al. 2018

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

show abstract

“…SUMO1 is a polypeptide composed of 101 amino acids, which mainly modifies proteins in physiological states; SUMO2 and SUMO3 are composed of 101 and 95 amino acids, respectively. SUMO2 and SUMO3 have 97% sequence homology to each other, however, they are only about 50% homologous compared with SUMO1 [ 32 ]. They mainly modify proteins related to stress response [ 33 ].…”

Section: The Dynamics Of Sumoylation In Hccmentioning

confidence: 99%

The Role of Protein SUMOylation in Human Hepatocellular Carcinoma: A Potential Target of New Drug Discovery and Development

Yuan

Zhang

et al. 2021

Cancers

View full text Add to dashboard Cite

Small ubiquitin-like modifier (SUMO) is a highly conserved post-translational modification protein, mainly found in eukaryotes. They are widely expressed in different tissues, including the liver. As an essential post-translational modification, SUMOylation is involved in many necessary regulations in cells. It plays a vital role in DNA repair, transcription regulation, protein stability and cell cycle progression. Increasing shreds of evidence show that SUMOylation is closely related to Hepatocellular carcinoma (HCC). The high expression of SUMOs in the inflammatory hepatic tissue may lead to the carcinogenesis of HCC. At the same time, SUMOs will upregulate the proliferation and survival of HCC, migration, invasion and metastasis of HCC, tumour microenvironment as well as drug resistance. This study reviewed the role of SUMOylation in liver cancer. In addition, it also discussed natural compounds that modulate SUMO and target SUMO drugs in clinical trials. Considering the critical role of SUMO protein in the occurrence of HCC, the drug regulation of SUMOylation may become a potential target for treatment, prognostic monitoring and adjuvant chemotherapy of HCC.

show abstract

“…In Arabidopsis, there are eight encoding genes of SUMO isoforms (AtSUMO), but only AtSUMO1, AtSUMO2, AtSUMO3, and AtSUMO5 are expressed [10,11]. Among them, AtSUMO1 and AtSUMO2, which share 83% sequence identity, are the highest expressed isoforms and double knock-out mutants sumo1sumo2 display embryo lethality [9,[12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Structural insights into SUMO E1–E2 interactions in Arabidopsis uncovers a distinctive platform for securing SUMO conjugation specificity across evolution

Liu

Lois

Reverter

2019

Biochemical Journal

View full text Add to dashboard Cite

SUMOylation of proteins involves the concerted action of the E1-activating enzyme, E2-conjugating enzyme and E3-ligases. An essential discrimination step in the SUMOylation pathway corresponds to the initial interaction between E1 ubiquitin-fold domain (UFD) and E2 enzymes. Although E2 orthologs possess high sequence identity, the E2 binding region of the UFD domains has diverged across evolution. Moreover, in reciprocal in vitro conjugation reactions Arabidopsis E1 and E2 SCE1 fail to interact efficiently with cognate human E2 Ubc9 and E1 partners, respectively. To gain more insights into the properties of this interface in evolutionary distant organisms, we solved the crystal structure of SUMO E2 SCE1 and its complex with E1 UFD in Arabidopsis. In addition to a few common structural determinants, the interface between the E1 UFD and E2 in Arabidopsis is distinct compared with human and yeast, in particular by the presence of a longer α-helix in the Arabidopsis UFD domain. Despite the variability of E1 UFD domains in these surfaces, they establish specific interactions with highly conserved surfaces of their cognate E2 enzymes. Functional analysis of the different E2 interface residues between human and Arabidopsis revealed Val37 (Met36 in human), as a determinant that provides specificity in the E1–E2 recognition in plants.

show abstract

SUMO Chain Formation by Plant Enzymes

Cited by 4 publications

References 4 publications

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

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

The Role of Protein SUMOylation in Human Hepatocellular Carcinoma: A Potential Target of New Drug Discovery and Development

Structural insights into SUMO E1–E2 interactions in Arabidopsis uncovers a distinctive platform for securing SUMO conjugation specificity across evolution

Contact Info

Product

Resources

About