TAILIEUCHUNG - Báo cáo khoa học: Identification, subcellular localization and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27

The natural transformation system of the thermophilic bacteriumThermus thermophilus HB27 comprises at least 16 distinct competence proteins enco-ded by seven distinct loci. In this article, we present for the first time biochemical analyses of the Thermus thermophiluscompetence proteins PilMNOWQ and PilA4, and demonstrate that thepilMNOWQgenes are each essential for natural transformation. | ềFEBS Journal Identification subcellular localization and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27 Judit Rumszauer Cornelia Schwarzenlander and Beate Averhoff Molecular Microbiology Bioenergetics Institute of Molecular Biosciences Johann Wolfgang Goethe University Frankfurt Main Germany Keywords pilus biogenesis Thermus thermophilus transformation competency Correspondence B. Averhoff Molecular Microbiology Bioenergetics Institute of Molecular Biosciences Johann Wolfgang Goethe University Frankfurt Main Campus Riedberg Max-von-Laue-Str. 9 60438 Frankfurt Germany Fax 49 69 79829306 Tel 49 69 79829509 E-mail Averhoff@ Received 10April2006 revised 17 May 2006 accepted 23 May 2006 doi The natural transformation system of the thermophilic bacterium Thermus thermophilus HB27 comprises at least 16 distinct competence proteins encoded by seven distinct loci. In this article we present for the first time biochemical analyses of the Thermus thermophilus competence proteins PilMNOWQ and PilA4 and demonstrate that the pilMNOWQ genes are each essential for natural transformation. We identified three different forms of PilA4 one with an apparent molecular mass of 14 kDa which correlates with that of the deduced protein an 18-kDa form and a 23-kDa form the last was found to be glycosylated. We demonstrate that PilM PilN and PilO are located in the inner membrane whereas PilW PilQ and PilA4 are located in the inner and outer membranes. These data show that PilMNOWQ and PilA4 are components of a DNA translocator structure that spans the inner and outer membranes. We further show that PilA4 and PilQ both copurify with pilus structures. Possible functions of PilQ and PilA4 in DNA translocation and in pilus biogenesis are discussed. Comparative mutant studies revealed that mutations in either pilW or pilQ .

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