Selection of a high-affinity DNA pool for a bZip protein with an out-of-phase alignment of the basic region relative to the leucine zipper

Young sam Lee; Daniel G. Gurnon; Jessica J. Hollenbeck; Martha G. Oakley

doi:10.1016/S0968-0896(01)00158-4

Selection of a high-affinity DNA pool for a bZip protein with an out-of-phase alignment of the basic region relative to the leucine zipper

Young sam Lee, Daniel G. Gurnon, Jessica J. Hollenbeck, Martha G. Oakley

Molecular and Cellular Biochemistry

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

Abstract

bZip transcription factors contain two regions that are required for DNA binding: a leucine zipper dimerization domain and a highly charged basic region that directly contacts DNA. The spacing between these subdomains is strictly conserved, and changes in this spacing result in a loss of function. Using an in vitro selection strategy, we have investigated the ability of a bZip protein with incorrect spacing between these two regions to bind specifically to DNA. Surprisingly, we find that although such a protein does not bind to its predicted site, it is possible to isolate a pool of DNAs that bind with very similar affinity to that of GCN4 for its optimum DNA site.

Original language	English
Pages (from-to)	2335-2339
Number of pages	5
Journal	Bioorganic and Medicinal Chemistry
Volume	9
Issue number	9
DOIs	https://doi.org/10.1016/S0968-0896(01)00158-4
State	Published - 2001

Bibliographical note

Funding Information:
This work was supported by Grant GM57571 from the National Institutes of Health and Grant 32029-G4 from the American Chemical Society Petroleum Research Fund.

Funding

This work was supported by Grant GM57571 from the National Institutes of Health and Grant 32029-G4 from the American Chemical Society Petroleum Research Fund.

Funders	Funder number
National Institutes of Health (NIH)	32029-G4
National Institute of General Medical Sciences	R01GM057571
American Chemical Society Petroleum Research Fund

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmaceutical Science
Drug Discovery
Clinical Biochemistry
Organic Chemistry

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abstract = "bZip transcription factors contain two regions that are required for DNA binding: a leucine zipper dimerization domain and a highly charged basic region that directly contacts DNA. The spacing between these subdomains is strictly conserved, and changes in this spacing result in a loss of function. Using an in vitro selection strategy, we have investigated the ability of a bZip protein with incorrect spacing between these two regions to bind specifically to DNA. Surprisingly, we find that although such a protein does not bind to its predicted site, it is possible to isolate a pool of DNAs that bind with very similar affinity to that of GCN4 for its optimum DNA site.",

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T1 - Selection of a high-affinity DNA pool for a bZip protein with an out-of-phase alignment of the basic region relative to the leucine zipper

AU - Lee, Young sam

AU - Gurnon, Daniel G.

AU - Hollenbeck, Jessica J.

AU - Oakley, Martha G.

N1 - Funding Information: This work was supported by Grant GM57571 from the National Institutes of Health and Grant 32029-G4 from the American Chemical Society Petroleum Research Fund.

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AB - bZip transcription factors contain two regions that are required for DNA binding: a leucine zipper dimerization domain and a highly charged basic region that directly contacts DNA. The spacing between these subdomains is strictly conserved, and changes in this spacing result in a loss of function. Using an in vitro selection strategy, we have investigated the ability of a bZip protein with incorrect spacing between these two regions to bind specifically to DNA. Surprisingly, we find that although such a protein does not bind to its predicted site, it is possible to isolate a pool of DNAs that bind with very similar affinity to that of GCN4 for its optimum DNA site.

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Selection of a high-affinity DNA pool for a bZip protein with an out-of-phase alignment of the basic region relative to the leucine zipper

Abstract

Bibliographical note

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ASJC Scopus subject areas

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