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Mol. Cells 2012; 33(2): 211-216

Published online February 29, 2012

https://doi.org/10.1007/s10059-012-0006-5

© The Korean Society for Molecular and Cellular Biology

A Mutational Study of Cnu Reveals Attractive Forces between Cnu and H-NS

Sang Hoon Yun1, Sang Chun Ji1,3, Heung Jin Jeon1, Xun Wang1, Younghoon Lee2, Byong-Seok Choi2, and Heon M. Lim1,*

1Department of Biology, College of Biological Sciences and Biotechnology, Chungnam National University, Daejeon 305-764, Korea, 2Department of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea, 3Present address: Department of Pharmacology and Clinical Pharmacology, Seoul National University College of Medicine and Hospital, Seoul 110-799, Korea

Correspondence to : *Correspondence: hmlim@cnu.ac.kr

Received: January 6, 2012; Accepted: January 9, 2012

Abstract

Cnu is a small 71-amino acid protein that complexes with H-NS and binds to a specific sequence in the replication origin of the E. coli chromosome. To understand the me-chanism of interaction between Cnu and H-NS, we used bacterial genetics to select and analyze Cnu variants that cannot complex with H-NS. Out of 2,000 colonies, 40 Cnu variants were identified. Most variants (82.5%) had a single mutation, but a few variants (17.5%) had double amino acid changes. An in vitro assay was used to identify Cnu variants that were truly defective in H-NS binding. The changes in these defective variants occurred exclusively at charged amino acids (Asp, Glu, or Lys) on the surface of the protein. We propose that the attractive force that governs the Cnu-H-NS interaction is an ionic bond, unlike the hydrophobic interaction that is the major attractive force in most proteins.

Keywords Cnu, DNA binding, H-NS, protein-protein interaction

Article

Research Article

Mol. Cells 2012; 33(2): 211-216

Published online February 29, 2012 https://doi.org/10.1007/s10059-012-0006-5

Copyright © The Korean Society for Molecular and Cellular Biology.

A Mutational Study of Cnu Reveals Attractive Forces between Cnu and H-NS

Sang Hoon Yun1, Sang Chun Ji1,3, Heung Jin Jeon1, Xun Wang1, Younghoon Lee2, Byong-Seok Choi2, and Heon M. Lim1,*

1Department of Biology, College of Biological Sciences and Biotechnology, Chungnam National University, Daejeon 305-764, Korea, 2Department of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea, 3Present address: Department of Pharmacology and Clinical Pharmacology, Seoul National University College of Medicine and Hospital, Seoul 110-799, Korea

Correspondence to:*Correspondence: hmlim@cnu.ac.kr

Received: January 6, 2012; Accepted: January 9, 2012

Abstract

Cnu is a small 71-amino acid protein that complexes with H-NS and binds to a specific sequence in the replication origin of the E. coli chromosome. To understand the me-chanism of interaction between Cnu and H-NS, we used bacterial genetics to select and analyze Cnu variants that cannot complex with H-NS. Out of 2,000 colonies, 40 Cnu variants were identified. Most variants (82.5%) had a single mutation, but a few variants (17.5%) had double amino acid changes. An in vitro assay was used to identify Cnu variants that were truly defective in H-NS binding. The changes in these defective variants occurred exclusively at charged amino acids (Asp, Glu, or Lys) on the surface of the protein. We propose that the attractive force that governs the Cnu-H-NS interaction is an ionic bond, unlike the hydrophobic interaction that is the major attractive force in most proteins.

Keywords: Cnu, DNA binding, H-NS, protein-protein interaction

Mol. Cells
Jan 31, 2023 Vol.46 No.1, pp. 1~67
COVER PICTURE
RNAs form diverse shapes and play multiple functions as central molecules of gene expression. In this special issue on RNA, seven minireviews illustrate how basic concepts and recent RNA biology findings are transformed into new and exciting RNA therapeutics.

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