Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella.
Homologues of the protein constituents of the Klebsiella pneumoniae (Klebsiella oxytoca) type II secreton (T2S), the Pseudomonas aeruginosa type IV pilus/fimbrium biogenesis machinery (T4P) and the Methanococcus voltae flagellum biogenesis machinery (Fla) have been identified. Known constituents of these systems include (1). a major prepilin (preflagellin), (2). several minor prepilins (preflagellins), (3). a prepilin (preflagellin) peptidase/methylase, (4). an ATPase, (5). a multispanning transmembrane (TM) protein, (6). an outer-membrane secretin (lacking in Fla) and (7). several functionally uncharacterized envelope proteins. Sequence and phylogenetic analyses led to the conclusion that, although many of the protein constituents are probably homologous, extensive sequence divergence during evolution clouds this homology so that a common ancestry can be established for all three types of systems for only two constituents, the ATPase and the TM protein. Sequence divergence of the individual T2S constituents has occurred at characteristic rates, apparently without shuffling of constituents between systems. The same is probably also true for the T4P and Fla systems. The family of ATPases is much larger than the family of TM proteins, and many ATPase homologues function in capacities unrelated to those considered here. Many phylogenetic clusters of the ATPases probably exhibit uniform function. Some of these have a corresponding TM protein homologue although others probably function without one. It is further shown that proteins that compose the different phylogenetic clusters in both the ATPase and the TM protein families exhibit unique structural characteristics that are of probable functional significance. The TM proteins are shown to have arisen by at least two dissimilar intragenic duplication events, one in the bacterial kingdom and one in the archaeal kingdom. The archaeal TM proteins are twice as large as the bacterial TM proteins, suggesting an oligomeric structure for the latter.
Peabody
Christopher R
CR
Division of Biological Sciences, University of California at San Diego, La Jolla, CA 92093-0116, USA.
Chung
Yong Joon
YJ
Division of Biological Sciences, University of California at San Diego, La Jolla, CA 92093-0116, USA.
Yen
Ming-Ren
MR
Division of Biological Sciences, University of California at San Diego, La Jolla, CA 92093-0116, USA.
Vidal-Ingigliardi
Dominique
D
Unité de Génétique Moléculaire, CNRS URA 2172, Institut Pasteur, 25 rue du Dr Roux, 75724 Paris, Cedex 15, France.
Pugsley
Anthony P
AP
Unité de Génétique Moléculaire, CNRS URA 2172, Institut Pasteur, 25 rue du Dr Roux, 75724 Paris, Cedex 15, France.
Saier
Milton H
MH
Division of Biological Sciences, University of California at San Diego, La Jolla, CA 92093-0116, USA.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000595:Amino Acid Sequence; D001105:Archaea / Q000145:classification / Q000502:physiology*; D019843:Archaeal Proteins / Q000378:metabolism*; D001419:Bacteria / Q000145:classification; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000378:metabolism*; D010861:Fimbriae, Bacterial / Q000502:physiology*; D005407:Flagella / Q000502:physiology*; D008969:Molecular Sequence Data; D010802:Phylogeny; D012984:Software
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D000251:Adenosine Triphosphatases