Characterization of the SUMO-binding activity of the myeloproliferative and mental retardation (MYM)-type zinc fingers in ZNF261 and ZNF198

SUMO-binding proteins interact with SUMO modified proteins to mediate a wide range of functional consequences. Here, we report the identification of a new SUMO-binding protein, ZNF261. Four human proteins including ZNF261, ZNF198, ZNF262, and ZNF258 contain a stretch of tandem zinc fingers called my...

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Bibliographic Details
Published in:PloS one 2014-08, Vol.9 (8), p.e105271-e105271
Main Authors: Guzzo, Catherine M, Ringel, Alison, Cox, Eric, Uzoma, Ijeoma, Zhu, Heng, Blackshaw, Seth, Wolberger, Cynthia, Matunis, Michael J
Format: Article
Language:English
Subjects:
Amino acids
Arsenic
Binding proteins
Biochemistry
Biology and life sciences
Biophysics
Cell Line, Tumor
Chemical properties
Deoxyribonucleic acid
DNA
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Equilibrium
Gene expression
Humans
Immunofluorescence
Immunoprecipitation
Intellectual disabilities
Localization
Medicine
Mental disorders
Microscopy
Microscopy, Fluorescence
Molecular biology
Neurosciences
Nuclear Proteins - chemistry
Nuclear Proteins - metabolism
Protein Binding
Proteins
Public health
Sumo
SUMO-1 Protein - metabolism
Transcription Factors - chemistry
Transcription Factors - metabolism
Zinc
Zinc finger proteins
Zinc Fingers
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Summary:SUMO-binding proteins interact with SUMO modified proteins to mediate a wide range of functional consequences. Here, we report the identification of a new SUMO-binding protein, ZNF261. Four human proteins including ZNF261, ZNF198, ZNF262, and ZNF258 contain a stretch of tandem zinc fingers called myeloproliferative and mental retardation (MYM)-type zinc fingers. We demonstrated that MYM-type zinc fingers from ZNF261 and ZNF198 are necessary and sufficient for SUMO-binding and that individual MYM-type zinc fingers function as SUMO-interacting motifs (SIMs). Our binding studies revealed that the MYM-type zinc fingers from ZNF261 and ZNF198 interact with the same surface on SUMO-2 recognized by the archetypal consensus SIM. We also present evidence that MYM-type zinc fingers in ZNF261 contain zinc, but that zinc is not required for SUMO-binding. Immunofluorescence microscopy studies using truncated fragments of ZNF198 revealed that MYM-type zinc fingers of ZNF198 are necessary for localization to PML-nuclear bodies (PML-NBs). In summary, our studies have identified and characterized the SUMO-binding activity of the MYM-type zinc fingers in ZNF261 and ZNF198.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0105271