Homology among DNA-binding proteins suggests use of a conserved super-secondary structure

The amino acid sequences of the repressor and cro proteins of phages λ, 434 and P22 are homologous, especially in a region in which repressor and λ cro have a similar α-helix–turn–α-helix secondary structure. Model-building studies indicate that this structure is important in DNA binding, and we sug...

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Bibliographic Details
Published in:Nature (London) 1982-07, Vol.298 (5873), p.447-451
Main Authors: Sauer, R. T, Yocum, R. R, Doolittle, R. F, Lewis, M, Pabo, C. O
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacteriophages
Biological Evolution
Carrier Proteins - analysis
cro repressor
DNA, Bacterial - metabolism
DNA-Binding Proteins
Humanities and Social Sciences
Models, Molecular
multidisciplinary
Nucleic Acid Conformation
phage 434
phage lambda
phage P22
Protein Conformation
Repressor Proteins - analysis
repressors
Science
Science (multidisciplinary)
Transcription Factors - analysis
Viral Proteins
Viral Regulatory and Accessory Proteins
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Summary:The amino acid sequences of the repressor and cro proteins of phages λ, 434 and P22 are homologous, especially in a region in which repressor and λ cro have a similar α-helix–turn–α-helix secondary structure. Model-building studies indicate that this structure is important in DNA binding, and we suggest it may be a common feature of many DNA-binding proteins.
ISSN:0028-0836
1476-4687
DOI:10.1038/298447a0