3-A Resolution Structure of a Protein with Histone-like Properties in Prokaryotes

Overview

Journal Nature

Specialty Science

Date 1984 Aug 2

PMID 6540370

Citations 90

Authors

I Tanaka

K Appelt

J Dijk

S W White

K S Wilson

Affiliations

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Abstract

The 3-A structure of DNA-binding protein II, which exhibits histone-like properties in bacteria, has been determined. The molecule is dimeric and appears to bind to the phosphate backbone of DNA through two symmetry-related arms. A mechanism by which the protein induces DNA supercoiling is proposed.

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Consensus protein engineering on the thermostable histone-like bacterial protein HUs significantly improves stability and DNA binding affinity.

Georgoulis A, Louka M, Mylonas S, Stavros P, Nounesis G, Vorgias C Extremophiles. 2020; 24(2):293-306.

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HU of Is Essential for the Preservation of DNA Supercoiling.

Ferrandiz M, Carreno D, Ayora S, Campa A Front Microbiol. 2018; 9:493.

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A specific single-stranded DNA induces a distinct conformational change in the nucleoid-associated protein HU.

Nishida Y, Ikeya T, Mikawa T, Inoue J, Ito Y, Shintani Y Biochem Biophys Rep. 2017; 8:318-324.

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