Differential binding of Sin3 interacting repressor domains to the PAH2 domain of Sin3A

Yuan Ping Pang; Ganesh A. Kumar; Jin San Zhang; Raul Urrutia

doi:10.1016/S0014-5793(03)00749-X

Differential binding of Sin3 interacting repressor domains to the PAH2 domain of Sin3A

Yuan Ping Pang, Ganesh A. Kumar, Jin San Zhang, Raul Urrutia

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

The Sin3 interacting domain (SID), originally described in the Mad family of repressors, is a novel transcriptional repressor domain that binds the PAH2 domain of corepressors Sin3A and Sin3B with high affinities. The conserved SID-like domains are reportedly present in five KLF proteins. However, the KLF SIDs and the Mad SIDs can be classified into two subtypes according to sequence similarity. Here, we report the finding from computational and experimental studies that the two subtypes of SID domains bind differentially to Sin3A. This finding offers insights into a mechanism of cell growth regulation by interactions of different subtypes of SID-containing repressor proteins with Sin3. It also provides the structural basis for developing selective modulators of Sin3.

Original language	English (US)
Pages (from-to)	108-112
Number of pages	5
Journal	FEBS Letters
Volume	548
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(03)00749-X
State	Published - Jul 31 2003

Keywords

KLF protein
KLF11
Mad1
SID
Transcription
Zinc finger protein

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(03)00749-X

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title = "Differential binding of Sin3 interacting repressor domains to the PAH2 domain of Sin3A",

abstract = "The Sin3 interacting domain (SID), originally described in the Mad family of repressors, is a novel transcriptional repressor domain that binds the PAH2 domain of corepressors Sin3A and Sin3B with high affinities. The conserved SID-like domains are reportedly present in five KLF proteins. However, the KLF SIDs and the Mad SIDs can be classified into two subtypes according to sequence similarity. Here, we report the finding from computational and experimental studies that the two subtypes of SID domains bind differentially to Sin3A. This finding offers insights into a mechanism of cell growth regulation by interactions of different subtypes of SID-containing repressor proteins with Sin3. It also provides the structural basis for developing selective modulators of Sin3.",

keywords = "KLF protein, KLF11, Mad1, SID, Transcription, Zinc finger protein",

author = "Pang, {Yuan Ping} and Kumar, {Ganesh A.} and Zhang, {Jin San} and Raul Urrutia",

note = "Funding Information: Supported by the DARPA (DAAD19-01-1-0322 to Y.-P.P.), the University of Minnesota Supercomputing Institute (Y.-P.P.), the NIH (DK52913 and DK56620 to R.U.), the Lustgarten Foundation for Pancreatic Cancer Research (to R.U.), and the Thompson-Mayo Postdoctoral Fellowship (to G.A.K.).",

year = "2003",

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doi = "10.1016/S0014-5793(03)00749-X",

language = "English (US)",

volume = "548",

pages = "108--112",

journal = "FEBS Letters",

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T1 - Differential binding of Sin3 interacting repressor domains to the PAH2 domain of Sin3A

AU - Pang, Yuan Ping

AU - Kumar, Ganesh A.

AU - Zhang, Jin San

AU - Urrutia, Raul

N1 - Funding Information: Supported by the DARPA (DAAD19-01-1-0322 to Y.-P.P.), the University of Minnesota Supercomputing Institute (Y.-P.P.), the NIH (DK52913 and DK56620 to R.U.), the Lustgarten Foundation for Pancreatic Cancer Research (to R.U.), and the Thompson-Mayo Postdoctoral Fellowship (to G.A.K.).

PY - 2003/7/31

Y1 - 2003/7/31

N2 - The Sin3 interacting domain (SID), originally described in the Mad family of repressors, is a novel transcriptional repressor domain that binds the PAH2 domain of corepressors Sin3A and Sin3B with high affinities. The conserved SID-like domains are reportedly present in five KLF proteins. However, the KLF SIDs and the Mad SIDs can be classified into two subtypes according to sequence similarity. Here, we report the finding from computational and experimental studies that the two subtypes of SID domains bind differentially to Sin3A. This finding offers insights into a mechanism of cell growth regulation by interactions of different subtypes of SID-containing repressor proteins with Sin3. It also provides the structural basis for developing selective modulators of Sin3.

AB - The Sin3 interacting domain (SID), originally described in the Mad family of repressors, is a novel transcriptional repressor domain that binds the PAH2 domain of corepressors Sin3A and Sin3B with high affinities. The conserved SID-like domains are reportedly present in five KLF proteins. However, the KLF SIDs and the Mad SIDs can be classified into two subtypes according to sequence similarity. Here, we report the finding from computational and experimental studies that the two subtypes of SID domains bind differentially to Sin3A. This finding offers insights into a mechanism of cell growth regulation by interactions of different subtypes of SID-containing repressor proteins with Sin3. It also provides the structural basis for developing selective modulators of Sin3.

KW - KLF protein

KW - KLF11

KW - Mad1

KW - SID

KW - Transcription

KW - Zinc finger protein

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U2 - 10.1016/S0014-5793(03)00749-X

DO - 10.1016/S0014-5793(03)00749-X

M3 - Article

C2 - 12885416

AN - SCOPUS:0041736054

SN - 0014-5793

VL - 548

SP - 108

EP - 112

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

Differential binding of Sin3 interacting repressor domains to the PAH2 domain of Sin3A

Abstract

Keywords

ASJC Scopus subject areas

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