Structure and role of coupling proteins in conjugal DNA transfer.
Type IV secretory systems are transmembrane bacterial multiprotein complexes. They are pivotal for conjugation, bacterial-induced plant tumour formation, toxin secretion and mammalian pathogen intracellular activity. These systems are involved in the spread of antibiotic resistance genes among bacteria by enabling conjugative DNA transfer. When such translocons transport DNA, they require the assistance of multimeric integral inner membrane proteins, the type IV coupling proteins. Its structural prototype is plasmid R388 TrwB protein, responsible for coupling the relaxosome with the DNA transport apparatus during bacterial conjugation. Its monomeric molecular structure is reminiscent of ring helicases and AAA ATPases. The quaternary structure is made up by six equivalent protomers featuring a flattened sphere resembling F1-ATPase, with a central channel traversing the particle, thus connecting cytoplasm and periplasm.
Gomis-Rüth
F Xavier
FX
Institut de Biologia Molecular de Barcelona, CSIC, Spain. xgrcri@ibmb.csic.es
de la Cruz
Fernando
F
Coll
Miquel
M
D001419:Bacteria / Q000235:genetics* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003227:Conjugation, Genetic; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D010957:Plasmids
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; C403125:trwB protein, E coli