The Tra domain of the lactococcal CluA surface protein is a unique domain that contributes to sex factor DNA transfer

Journal of Bacteriology
Régis StentzC Shearman

Abstract

CluA is a cell surface-presented protein that causes cell aggregation and is essential for a high-efficiency conjugation process in Lactococcus lactis. We know from previous work that in addition to promoting cell-to-cell contact, CluA is involved in sex factor DNA transfer. To define the CluA domains involved in aggregation and in transfer, we first performed random mutagenesis of the cluA gene using a modified mini-Tn7 element which generated five amino acid insertions located throughout the encoded protein. Thirty independent cluA insertion mutants expressing modified CluA proteins at the cell surface were isolated and characterized further. The level of aggregation of each mutant was determined. The cell binding capacity of CluA was affected strongly when the protein had a mutation in its N-terminal region, which defined an aggregation domain extending from amino acid 153 to amino acid 483. Of the cluA mutants that still exhibited aggregation, eight showed an attenuated ability to conjugate, and six mutations were located in a 300-amino-acid C-terminal region of the protein defining a transfer domain (Tra). This result was confirmed by a phenotypic analysis of an additional five mutants obtained using site-directed mutagene...Continue Reading

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Aug 4, 2004·Microbiology·Régis StentzClaire Shearman

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Citations

Mar 17, 2010·Applied and Environmental Microbiology·Régis StentzClaire Shearman
Sep 11, 2012·Applied and Environmental Microbiology·Jovanka LukićJelena Begović
Mar 17, 2009·Applied and Environmental Microbiology·Jakob HaaberKarin Hammer
Jul 2, 2010·Survey of Ophthalmology·Ron Gutmark, David L Guyton
Apr 26, 2019·Frontiers in Microbiology·Philip KelleherDouwe van Sinderen
Dec 17, 2020·Frontiers in Microbiology·Michael A JärvåRonnie P-A Berntsson

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