Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO

Kirstin Keusekotten; Veronika N Bade; Katrin Meyer-Teschendorf; Annie Miriam Sriramachandran; Katrin Fischer-Schrader; Anke Krause; Christiane Horst; Günter Schwarz; Kay Hofmann; R Jürgen Dohmen; Gerrit J K Praefcke

doi:10.1042/BJ20130753

Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO

Biochem J. 2014 Jan 1;457(1):207-14. doi: 10.1042/BJ20130753.

Authors

Kirstin Keusekotten¹, Veronika N Bade, Katrin Meyer-Teschendorf, Annie Miriam Sriramachandran, Katrin Fischer-Schrader, Anke Krause, Christiane Horst, Günter Schwarz, Kay Hofmann, R Jürgen Dohmen, Gerrit J K Praefcke

Affiliation

¹ †Institute for Genetics, University of Cologne, 50674 Köln, Germany.

Abstract

RNF4 (RING finger protein 4) is a STUbL [SUMO (small ubiquitin-related modifier)-targeted ubiquitin ligase] controlling PML (promyelocytic leukaemia) nuclear bodies, DNA double strand break repair and other nuclear functions. In the present paper, we describe that the sequence and spacing of the SIMs (SUMO-interaction motifs) in RNF4 regulate the avidity-driven recognition of substrate proteins carrying SUMO chains of variable length.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Binding Sites
HeLa Cells
Humans
Molecular Sequence Data
Nuclear Proteins / chemistry*
Nuclear Proteins / metabolism*
Protein Binding / physiology
Protein Interaction Domains and Motifs* / physiology
SUMO-1 Protein / metabolism*
Saccharomyces cerevisiae
Substrate Specificity
Sumoylation / physiology*
Transcription Factors / chemistry*
Transcription Factors / metabolism*

Substances

Nuclear Proteins
RNF4 protein, human
SUMO-1 Protein
Transcription Factors