Phage display is a useful means of identifying and selecting proteins of interest that bind specific targets. In order to examine the potential of phage display for the genome-wide screening of DNA-binding proteins, we constructed yeast genomic libraries using lambda foo-based vectors devised in this work. After affinity selection using GAL4 UAS(G) as a probe, phages expressing GAL4 were enriched approximately 5 x 10(5)-fold from the library. Approximately 90% of polypeptides encoded in correct translation reading frames by the selected phages were known or putative polynucleotide-binding proteins. This result clearly indicates that the modified lambda phage display vector in combination with our enrichment technique has great potential for the enrichment of DNA-binding proteins in a sequence-specific manner.
Affinity selection of DNA-binding proteins from yeast genomic DNA libraries by improved lambda phage display vector. Publishing Authors By Initials
Affinity selection of DNA-binding proteins from yeast genomic DNA libraries by improved lambda phage display vector. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Journal of biochemistry
VOLUME: 132
Page Numbers: 975-82
Journal Abbreviation: J. Biochem.
ISSN: 0021-924X
DAY: 19
MONTH: Dec
YEAR: 2002
Affinity selection of DNA-binding proteins from yeast genomic DNA libraries by improved lambda phage display vector. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 376600
Affinity selection of DNA-binding proteins from yeast genomic DNA libraries by improved lambda phage display vector. Keywords Mesh Terms:
KEYWORDS: Transcription Factors
MESH TERMS: metabolism
Chemical & Substance for Abstract: Affinity selection of DNA-binding proteins from yeast genomic DNA libraries by improved lambda phage display vector. Information
Substance Name: Transcription Factors
Registry Number: 0
Grant and Affiliation Information for Affinity selection of DNA-binding proteins from yeast genomic DNA libraries by improved lambda phage display vector.
AFFILIATION: Research Center for Glycoscience, Advanced Institute of Industrial Science and Technology, Central Higashi, Tsukuba, Ibaraki 305-8566, Japan.
Country: Japan
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MEDLINETA: J Biochem
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