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Structure of the DNA binding wing of the gene‐V encoded single‐stranded DNA binding protein of the filamentous bacteriophage M13
Author(s) -
van Duynhoven J.P.M.,
Folkers P.J.M.,
Stassen A.P.M.,
Harmsen B.J.M.,
Konings R.N.H.,
Hilbers C.W.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80621-o
Subject(s) - filamentous bacteriophage , dna , hmg box , biology , protein–dna interaction , gene , replication protein a , dna binding protein , microbiology and biotechnology , in vitro recombination , dna binding site , genetics , bacteriophage , peptide sequence , gene expression , transcription factor , promoter , molecular cloning , escherichia coli
The structure in solution of a β‐loop in mutant Y41H of the single‐stranded DNA binding protein encoded by gene‐V of the filamentous phage M13 has been elucidated using 2‐dimensional 1 H‐nuclear magnetic resonance techniques. Furthermore, these studies enabled us to demonstrate that an identical structural element is present in wild‐type gene‐V‐protein and that this element intimately is involved in the binding of gene‐V‐protein to single‐stranded DNA. It is shown that the structure of the DNA binding wing deviates from that proposed for the same amino acid sequence on the basis of X‐ray diffraction data. The structure is, however, identical to that of the DNA binding wing present in the single‐stranded DNA binding protein encoded by the genome of the evolutionary distantly related filamentous phage IKe. The latter observations support our current view that in the binding of these proteins to single‐stranded DNA a common structural motif is involved.