Premium
Structural similarities and differences in H‐ NS family proteins revealed by the N‐terminal structure of TurB in Pseudomonas putida KT 2440
Author(s) -
SuzukiMinakuchi Chiho,
Kawazuma Kohei,
Matsuzawa Jun,
Vasileva Delyana,
Fujimoto Zui,
Terada Tohru,
Okada Kazunori,
Nojiri Hideaki
Publication year - 2016
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 - 10.1002/1873-3468.12425
Subject(s) - pseudomonas putida , escherichia coli , nucleoid , peptide sequence , pseudomonas , stereochemistry , chemistry , biology , biochemistry , bacteria , genetics , gene
H‐ NS family proteins play key roles in bacterial nucleoid compaction and global transcription. MvaT homologues in Pseudomonas have almost negligible amino acid sequence identity with H‐ NS , but can complement an hns ‐related phenotype of Escherichia coli . Here, we report the crystal structure of the N‐terminal dimerization/oligomerization domain of TurB, an MvaT homologue in Pseudomonas putida KT 2440. Our data identify two dimerization sites; the structure of the central dimerization site is almost the same as the corresponding region of H‐ NS , whereas the terminal dimerization sites are different. Our results reveal similarities and differences in dimerization and oligomerization mechanisms between H‐ NS and TurB.