Proteins with two SUMO-like domains in chromatin-associated complexes: The RENi (Rad60-Esc2-NIP45) family

<p>Abstract</p> <p>Background</p> <p>Post-translational modification by Small Ubiquitin-like Modifiers (SUMO) has been implicated in protein targeting, in the maintenance of genomic integrity and in transcriptional control. But the specific molecular effects of SUMO mod...

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Main Authors: Eisenhaber Birgit, Bachmair Andreas, Novatchkova Maria, Eisenhaber Frank
Format: Article
Language:English
Published: BMC 2005-02-01
Series:BMC Bioinformatics
Online Access:http://www.biomedcentral.com/1471-2105/6/22
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author Eisenhaber Birgit
Bachmair Andreas
Novatchkova Maria
Eisenhaber Frank
author_facet Eisenhaber Birgit
Bachmair Andreas
Novatchkova Maria
Eisenhaber Frank
author_sort Eisenhaber Birgit
collection DOAJ
description <p>Abstract</p> <p>Background</p> <p>Post-translational modification by Small Ubiquitin-like Modifiers (SUMO) has been implicated in protein targeting, in the maintenance of genomic integrity and in transcriptional control. But the specific molecular effects of SUMO modification on many target proteins remain to be elucidated. Recent findings point at the importance of SUMO-mediated histone NAD-dependent deacetylase (HDAC) recruitment in transcriptional regulation.</p> <p>Results</p> <p>We describe the RENi family of SUMO-like domain proteins (SDP) with the unique feature of typically containing two carboxy-terminal SUMO-like domains. Using sequence analytic evidence, we collect family members from animals, fungi and plants, most prominent being yeast <b>R</b>ad60, <b>E</b>sc2 and mouse <b>NI</b>P45 <url>http://mendel.imp.univie.ac.at/SEQUENCES/reni/</url>. Different proteins of the novel family are known to interact directly with histone NAD-dependent deacetylases (HDACs), structural maintenance of chromosomes (SMC) proteins, and transcription factors. In particular, the highly non-trivial designation of the first of the two successive SUMO-domains in non-plant RENi provides a rationale for previously published functionally impaired mutant variants.</p> <p>Conclusions</p> <p>Till now, SUMO-like proteins have been studied exclusively in the context of their covalent conjugation to target proteins. Here, we present the exciting possibility that SUMO domain proteins, similarly to ubiquitin modifiers, have also evolved in a second line – namely as multi-domain proteins that are non-covalently attached to their target proteins. We suggest that the SUMO stable fusion proteins of the RENi family, which we introduce in this work, might mimic SUMO and share its interaction motifs (in analogy to the way that ubiquitin-like domains mimic ubiquitin). This presumption is supported by parallels in the spectrum of modified or bound proteins e.g. transcription factors and chromatin-associated proteins and in the recruitment of HDAC-activity.</p>
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spelling doaj.art-49856149b90a47b18e0d52e4f0756d492022-12-21T21:04:10ZengBMCBMC Bioinformatics1471-21052005-02-01612210.1186/1471-2105-6-22Proteins with two SUMO-like domains in chromatin-associated complexes: The RENi (Rad60-Esc2-NIP45) familyEisenhaber BirgitBachmair AndreasNovatchkova MariaEisenhaber Frank<p>Abstract</p> <p>Background</p> <p>Post-translational modification by Small Ubiquitin-like Modifiers (SUMO) has been implicated in protein targeting, in the maintenance of genomic integrity and in transcriptional control. But the specific molecular effects of SUMO modification on many target proteins remain to be elucidated. Recent findings point at the importance of SUMO-mediated histone NAD-dependent deacetylase (HDAC) recruitment in transcriptional regulation.</p> <p>Results</p> <p>We describe the RENi family of SUMO-like domain proteins (SDP) with the unique feature of typically containing two carboxy-terminal SUMO-like domains. Using sequence analytic evidence, we collect family members from animals, fungi and plants, most prominent being yeast <b>R</b>ad60, <b>E</b>sc2 and mouse <b>NI</b>P45 <url>http://mendel.imp.univie.ac.at/SEQUENCES/reni/</url>. Different proteins of the novel family are known to interact directly with histone NAD-dependent deacetylases (HDACs), structural maintenance of chromosomes (SMC) proteins, and transcription factors. In particular, the highly non-trivial designation of the first of the two successive SUMO-domains in non-plant RENi provides a rationale for previously published functionally impaired mutant variants.</p> <p>Conclusions</p> <p>Till now, SUMO-like proteins have been studied exclusively in the context of their covalent conjugation to target proteins. Here, we present the exciting possibility that SUMO domain proteins, similarly to ubiquitin modifiers, have also evolved in a second line – namely as multi-domain proteins that are non-covalently attached to their target proteins. We suggest that the SUMO stable fusion proteins of the RENi family, which we introduce in this work, might mimic SUMO and share its interaction motifs (in analogy to the way that ubiquitin-like domains mimic ubiquitin). This presumption is supported by parallels in the spectrum of modified or bound proteins e.g. transcription factors and chromatin-associated proteins and in the recruitment of HDAC-activity.</p>http://www.biomedcentral.com/1471-2105/6/22
spellingShingle Eisenhaber Birgit
Bachmair Andreas
Novatchkova Maria
Eisenhaber Frank
Proteins with two SUMO-like domains in chromatin-associated complexes: The RENi (Rad60-Esc2-NIP45) family
BMC Bioinformatics
title Proteins with two SUMO-like domains in chromatin-associated complexes: The RENi (Rad60-Esc2-NIP45) family
title_full Proteins with two SUMO-like domains in chromatin-associated complexes: The RENi (Rad60-Esc2-NIP45) family
title_fullStr Proteins with two SUMO-like domains in chromatin-associated complexes: The RENi (Rad60-Esc2-NIP45) family
title_full_unstemmed Proteins with two SUMO-like domains in chromatin-associated complexes: The RENi (Rad60-Esc2-NIP45) family
title_short Proteins with two SUMO-like domains in chromatin-associated complexes: The RENi (Rad60-Esc2-NIP45) family
title_sort proteins with two sumo like domains in chromatin associated complexes the reni rad60 esc2 nip45 family
url http://www.biomedcentral.com/1471-2105/6/22
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