SUMO-1 Modification Regulates the DNA Binding Activity of Heat Shock Transcription Factor 2, a Promyelocytic Leukemia Nuclear Body Associated Transcription Factor

Michael L. Goodson, Yiling Hong, Richard Rogers, Michael J Matunis, Ok Kyong Park-Sargell, Kevin D. Sarge

Research output: Contribution to journalArticle

Abstract

Heat shock transcription factor 2 (HSF2) is a transcription factor that regulates heat shock protein gene expression, but the mechanisms regulating the function of this factor are unclear. Here we report that HSF2 is a substrate for modification by the ubiquitin-related protein SUMO-1 and that HSF2 colocalizes in cells with SUMO-1 in nuclear granules. Staining with anti-promyelocytic leukemia antibodies indicates that these HSF2-containing nuclear granules are PML bodies. Our results identify lysine 82 as the major site of SUMO-1 modification in HSF2, which is located in a "wing" within the DNA-binding domain of this protein. Interestingly, SUMO-1 modification of HSF2 results in conversion of this factor to the active DNA binding form. This is the first demonstration that SUMO-1 modification can directly alter the DNA binding ability of a transcription factor and reveals a new mechanism by which SUMO-1 modification can regulate protein function.

Original languageEnglish (US)
Pages (from-to)18513-18518
Number of pages6
JournalJournal of Biological Chemistry
Volume276
Issue number21
DOIs
StatePublished - Jan 25 2001

Fingerprint

Leukemia
Transcription Factors
DNA
SUMO-1 Protein
DNA-Binding Proteins
Ubiquitin
Heat-Shock Proteins
Gene expression
Lysine
heat shock transcription factor
Proteins
Demonstrations
Staining and Labeling
Gene Expression
Antibodies
Substrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

SUMO-1 Modification Regulates the DNA Binding Activity of Heat Shock Transcription Factor 2, a Promyelocytic Leukemia Nuclear Body Associated Transcription Factor. / Goodson, Michael L.; Hong, Yiling; Rogers, Richard; Matunis, Michael J; Park-Sargell, Ok Kyong; Sarge, Kevin D.

In: Journal of Biological Chemistry, Vol. 276, No. 21, 25.01.2001, p. 18513-18518.

Research output: Contribution to journalArticle

Goodson, Michael L. ; Hong, Yiling ; Rogers, Richard ; Matunis, Michael J ; Park-Sargell, Ok Kyong ; Sarge, Kevin D. / SUMO-1 Modification Regulates the DNA Binding Activity of Heat Shock Transcription Factor 2, a Promyelocytic Leukemia Nuclear Body Associated Transcription Factor. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 21. pp. 18513-18518.
@article{00451a62c9754ce688166df99d8d053d,
title = "SUMO-1 Modification Regulates the DNA Binding Activity of Heat Shock Transcription Factor 2, a Promyelocytic Leukemia Nuclear Body Associated Transcription Factor",
abstract = "Heat shock transcription factor 2 (HSF2) is a transcription factor that regulates heat shock protein gene expression, but the mechanisms regulating the function of this factor are unclear. Here we report that HSF2 is a substrate for modification by the ubiquitin-related protein SUMO-1 and that HSF2 colocalizes in cells with SUMO-1 in nuclear granules. Staining with anti-promyelocytic leukemia antibodies indicates that these HSF2-containing nuclear granules are PML bodies. Our results identify lysine 82 as the major site of SUMO-1 modification in HSF2, which is located in a {"}wing{"} within the DNA-binding domain of this protein. Interestingly, SUMO-1 modification of HSF2 results in conversion of this factor to the active DNA binding form. This is the first demonstration that SUMO-1 modification can directly alter the DNA binding ability of a transcription factor and reveals a new mechanism by which SUMO-1 modification can regulate protein function.",
author = "Goodson, {Michael L.} and Yiling Hong and Richard Rogers and Matunis, {Michael J} and Park-Sargell, {Ok Kyong} and Sarge, {Kevin D.}",
year = "2001",
month = "1",
day = "25",
doi = "10.1074/jbc.M008066200",
language = "English (US)",
volume = "276",
pages = "18513--18518",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "21",

}

TY - JOUR

T1 - SUMO-1 Modification Regulates the DNA Binding Activity of Heat Shock Transcription Factor 2, a Promyelocytic Leukemia Nuclear Body Associated Transcription Factor

AU - Goodson, Michael L.

AU - Hong, Yiling

AU - Rogers, Richard

AU - Matunis, Michael J

AU - Park-Sargell, Ok Kyong

AU - Sarge, Kevin D.

PY - 2001/1/25

Y1 - 2001/1/25

N2 - Heat shock transcription factor 2 (HSF2) is a transcription factor that regulates heat shock protein gene expression, but the mechanisms regulating the function of this factor are unclear. Here we report that HSF2 is a substrate for modification by the ubiquitin-related protein SUMO-1 and that HSF2 colocalizes in cells with SUMO-1 in nuclear granules. Staining with anti-promyelocytic leukemia antibodies indicates that these HSF2-containing nuclear granules are PML bodies. Our results identify lysine 82 as the major site of SUMO-1 modification in HSF2, which is located in a "wing" within the DNA-binding domain of this protein. Interestingly, SUMO-1 modification of HSF2 results in conversion of this factor to the active DNA binding form. This is the first demonstration that SUMO-1 modification can directly alter the DNA binding ability of a transcription factor and reveals a new mechanism by which SUMO-1 modification can regulate protein function.

AB - Heat shock transcription factor 2 (HSF2) is a transcription factor that regulates heat shock protein gene expression, but the mechanisms regulating the function of this factor are unclear. Here we report that HSF2 is a substrate for modification by the ubiquitin-related protein SUMO-1 and that HSF2 colocalizes in cells with SUMO-1 in nuclear granules. Staining with anti-promyelocytic leukemia antibodies indicates that these HSF2-containing nuclear granules are PML bodies. Our results identify lysine 82 as the major site of SUMO-1 modification in HSF2, which is located in a "wing" within the DNA-binding domain of this protein. Interestingly, SUMO-1 modification of HSF2 results in conversion of this factor to the active DNA binding form. This is the first demonstration that SUMO-1 modification can directly alter the DNA binding ability of a transcription factor and reveals a new mechanism by which SUMO-1 modification can regulate protein function.

UR - http://www.scopus.com/inward/record.url?scp=0035947677&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035947677&partnerID=8YFLogxK

U2 - 10.1074/jbc.M008066200

DO - 10.1074/jbc.M008066200

M3 - Article

C2 - 11278381

AN - SCOPUS:0035947677

VL - 276

SP - 18513

EP - 18518

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 21

ER -