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N terminus determinants of MinC from Neisseria gonorrhoeae mediate interaction with FtsZ but do not affect interaction with MinD or homodimerization

N terminus determinants of MinC from Neisseria gonorrhoeae mediate interaction with FtsZ but do... While bacterial cell division has been widely studied in rod-shaped bacteria, the mechanism of cell division in round (coccal) bacteria remains largely enigmatic. In the present study, interaction between the cell division inhibitor MinC from Neisseria gonorrhoeae (MinC Ng ) and the gonococcal cell division proteins MinD Ng and FtsZ Ng are demonstrated. Protein truncation and site-directed mutagenic approaches determined which N-terminal residues were essential for cell division inhibition by MinC Ng using cell morphology as an indicator of protein functionality. Truncation from or mutation at the 13th amino acid of the N terminus of MinC Ng resulted in loss of protein function. Bioinformatic analyses predicted that point mutations of L35P and L68P would affect the α-helical conformation of the protein and we experimentally showed that these mutations alter the functionality of MinC Ng . The bacterial two-hybrid system showed that interaction of MinC Ng with FtsZ Ng is abrogated upon truncation of 13 N-terminal residues while MinC Ng -MinD Ng interaction or MinC Ng homodimerization is unaffected. These data confirm interactions among gonococcal cell division proteins and determine the necessity of the 13th amino acid for MinC Ng function. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

N terminus determinants of MinC from Neisseria gonorrhoeae mediate interaction with FtsZ but do not affect interaction with MinD or homodimerization

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References (22)

Publisher
Springer Journals
Copyright
Copyright © 2007 by Springer-Verlag
Subject
Life Sciences; Ecology; Biotechnology; Cell Biology; Biochemistry, general; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/s00203-007-0210-4
pmid
17287984
Publisher site
See Article on Publisher Site

Abstract

While bacterial cell division has been widely studied in rod-shaped bacteria, the mechanism of cell division in round (coccal) bacteria remains largely enigmatic. In the present study, interaction between the cell division inhibitor MinC from Neisseria gonorrhoeae (MinC Ng ) and the gonococcal cell division proteins MinD Ng and FtsZ Ng are demonstrated. Protein truncation and site-directed mutagenic approaches determined which N-terminal residues were essential for cell division inhibition by MinC Ng using cell morphology as an indicator of protein functionality. Truncation from or mutation at the 13th amino acid of the N terminus of MinC Ng resulted in loss of protein function. Bioinformatic analyses predicted that point mutations of L35P and L68P would affect the α-helical conformation of the protein and we experimentally showed that these mutations alter the functionality of MinC Ng . The bacterial two-hybrid system showed that interaction of MinC Ng with FtsZ Ng is abrogated upon truncation of 13 N-terminal residues while MinC Ng -MinD Ng interaction or MinC Ng homodimerization is unaffected. These data confirm interactions among gonococcal cell division proteins and determine the necessity of the 13th amino acid for MinC Ng function.

Journal

Archives of MicrobiologySpringer Journals

Published: Jun 1, 2007

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