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All three J‐domain proteins of the Escherichia coli DnaK chaperone machinery are DNA binding proteins
Author(s) -
Gur Eyal,
Katz Chen,
Ron Eliora Z.
Publication year - 2005
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/j.febslet.2005.01.084
Subject(s) - escherichia coli , dna , chaperone (clinical) , dna binding protein , single stranded binding protein , biology , biochemistry , binding domain , dna binding domain , membrane protein , telomere binding protein , cytoplasm , microbiology and biotechnology , binding site , gene , transcription factor , membrane , medicine , pathology
DnaJ, DjlA and CbpA are the J‐domain proteins of DnaK, the major Hsp70 of Escherichia coli . CbpA was originally discovered as a DNA binding protein. Here, we show that DNA binding is a property of DnaJ and DjlA as well. Of special interest in this respect is DjlA, as this cytoplasmic protein is membrane bound and, as shown here, its affinity for DNA is extremely high. The finding that all the three J‐proteins of DnaK are DNA binding proteins sheds new light on the cellular activity of these proteins.