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Purification and Characterization of a DNA-binding protein for Nucleoid Structure of Escherichia coli

山口医学 Volume 31 Issue 3 Page 319-328
published_at 1982-06
Title
大腸菌の核様体構成蛋白の精製とその性質
Purification and Characterization of a DNA-binding protein for Nucleoid Structure of Escherichia coli
Creators Kishi Fumio
Source Identifiers
A 22,000-dalton DNA-binding protein has been purified to apparent homogeneity from the cells of an Escherichia coli K-12 strain. The protein binds to the superhelical DNA molecule with a protein to DNA weight ratio of 3 to 2. The protein showed the high affinity to the single-stranded DNA molecule and the lower affinity to the linear duplex DNA molecule. The amino acid composition of the protein resembled those of the other prokaryotic histone-like proteins and eukaryotic histone H2A. The protein was heat labile unlike other histone-like proteins. In addition, DNA, RNA and protein syntheses in vitro were not affected by the presence of the protein. In view of these features, this protein may play a role in maintaining the bacterial nucleoid structure.
Subjects
医学 ( Other)
Languages jpn
Resource Type journal article
Publishers 山口大学医学会
Date Issued 1982-06
File Version Not Applicable (or Unknown)
Access Rights metadata only access
Relations
[ISSN]0513-1731
[NCID]AN00243156
Schools 医学部