title: Functional organization of MobB, a small protein required for efficient conjugal transfer of plasmid R1162.
abstract: MobB is a small (molecular weight = 15,097) protein encoded by the broad-host-range plasmid R1162 and is required for its efficient transfer by conjugation. The C-terminal half of the protein contains a membrane domain essential for transfer. This region can be replaced by a putative membrane domain from another, unrelated protein, and thus is likely to function independently from the rest of MobB. The other, functionally active region of MobB, identified by mutagenesis, is at the N-terminal end. One mutation affecting this region inhibits replication, suggesting that this part of the protein is contacting and sequestering the relaxase-linked primase. The overall organization reflects a multimeric and bipolar organization, with molecules of MobB anchored in the membrane at one end and engaging the relaxase at the other. This arrangement could increase the transfer frequency by raising the probability of contact between the relaxase and the membrane-embedded, coupling protein for type IV secretion.
authors.affiliation: Section of Molecular Genetics and Microbiology, Institute of Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA. rmeyer@mail.utexas.edu
authors.forename: Richard
authors.initials: R
authors.lastname: Meyer
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D003227:Conjugation, Genetic; D048168:Escherichia coli K12 / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010957:Plasmids / Q000235:genetics*
chemical_list: D029968:Escherichia coli Proteins; C490938:MobB protein, E coli