Recognition of DNA sequences by the repressor of bacteriophage 434

S. C. Harrison; J. E. Anderson; G. B. Koudelka; A. Mondragon; S. Subbiah; R. P. Wharton; C. Wolberger; M. Ptashne

doi:10.1016/0301-4622(88)87022-4

Recognition of DNA sequences by the repressor of bacteriophage 434

S. C. Harrison^*, J. E. Anderson, G. B. Koudelka, A. Mondragon, S. Subbiah, R. P. Wharton, C. Wolberger, M. Ptashne

^*Corresponding author for this work

Molecular Biosciences

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

9 Scopus citations

Abstract

The structure of a complex between the DNA-binding domain of phase 434 repressor and a 14 base-pair synthetic DNA operator reveals the molecular interactions important far sequence-specific recognition A set of contacts with DNA backbone, notably involving hydrogen bonds between peptide -NH groups and DNA phosphates, position the repressor and fix the DNA configurations. Direct interactions between amino acid side chains and DNA bases involve nonpolar van der Waals contacts as well as hydrogen bonds. The structures of the repressor domain and of the 434 cro protein are extremely similar. There appear to be no major conformational changes in the proteins when they bind to DNA.

Original language	English (US)
Pages (from-to)	31-37
Number of pages	7
Journal	Biophysical Chemistry
Volume	29
Issue number	1-2
DOIs	https://doi.org/10.1016/0301-4622(88)87022-4
State	Published - Feb 1988

Keywords

DNA sequence recognition
DNA-protein binding
Repressor-operator complex
Transcriptional regulation
X-ray crystallography

ASJC Scopus subject areas

Biophysics
Biochemistry
Organic Chemistry

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10.1016/0301-4622(88)87022-4

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title = "Recognition of DNA sequences by the repressor of bacteriophage 434",

abstract = "The structure of a complex between the DNA-binding domain of phase 434 repressor and a 14 base-pair synthetic DNA operator reveals the molecular interactions important far sequence-specific recognition A set of contacts with DNA backbone, notably involving hydrogen bonds between peptide -NH groups and DNA phosphates, position the repressor and fix the DNA configurations. Direct interactions between amino acid side chains and DNA bases involve nonpolar van der Waals contacts as well as hydrogen bonds. The structures of the repressor domain and of the 434 cro protein are extremely similar. There appear to be no major conformational changes in the proteins when they bind to DNA.",

keywords = "DNA sequence recognition, DNA-protein binding, Repressor-operator complex, Transcriptional regulation, X-ray crystallography",

author = "Harrison, {S. C.} and Anderson, {J. E.} and Koudelka, {G. B.} and A. Mondragon and S. Subbiah and Wharton, {R. P.} and C. Wolberger and M. Ptashne",

note = "Funding Information: This work was supported by NIH grant GM-29109. J.E.A. was a Burroughs-Wellcome Fellow of the Life Sciences Research Foundation and G.B.K. and A.M. were Fellows of the Damon Runyon-Walter Winchell Cancer Fund.",

year = "1988",

month = feb,

doi = "10.1016/0301-4622(88)87022-4",

language = "English (US)",

volume = "29",

pages = "31--37",

journal = "Biophysical Chemistry",

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T1 - Recognition of DNA sequences by the repressor of bacteriophage 434

AU - Harrison, S. C.

AU - Anderson, J. E.

AU - Koudelka, G. B.

AU - Mondragon, A.

AU - Subbiah, S.

AU - Wharton, R. P.

AU - Wolberger, C.

AU - Ptashne, M.

N1 - Funding Information: This work was supported by NIH grant GM-29109. J.E.A. was a Burroughs-Wellcome Fellow of the Life Sciences Research Foundation and G.B.K. and A.M. were Fellows of the Damon Runyon-Walter Winchell Cancer Fund.

PY - 1988/2

Y1 - 1988/2

N2 - The structure of a complex between the DNA-binding domain of phase 434 repressor and a 14 base-pair synthetic DNA operator reveals the molecular interactions important far sequence-specific recognition A set of contacts with DNA backbone, notably involving hydrogen bonds between peptide -NH groups and DNA phosphates, position the repressor and fix the DNA configurations. Direct interactions between amino acid side chains and DNA bases involve nonpolar van der Waals contacts as well as hydrogen bonds. The structures of the repressor domain and of the 434 cro protein are extremely similar. There appear to be no major conformational changes in the proteins when they bind to DNA.

AB - The structure of a complex between the DNA-binding domain of phase 434 repressor and a 14 base-pair synthetic DNA operator reveals the molecular interactions important far sequence-specific recognition A set of contacts with DNA backbone, notably involving hydrogen bonds between peptide -NH groups and DNA phosphates, position the repressor and fix the DNA configurations. Direct interactions between amino acid side chains and DNA bases involve nonpolar van der Waals contacts as well as hydrogen bonds. The structures of the repressor domain and of the 434 cro protein are extremely similar. There appear to be no major conformational changes in the proteins when they bind to DNA.

KW - DNA sequence recognition

KW - DNA-protein binding

KW - Repressor-operator complex

KW - Transcriptional regulation

KW - X-ray crystallography

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DO - 10.1016/0301-4622(88)87022-4

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SN - 0301-4622

VL - 29

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EP - 37

JO - Biophysical Chemistry

JF - Biophysical Chemistry

IS - 1-2

ER -

Recognition of DNA sequences by the repressor of bacteriophage 434

Abstract

Keywords

ASJC Scopus subject areas

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