Open AccessPhylogenetic and structural analyses of the oxa1 family of protein translocases
Author(s) -
Yen MingRen,
Harley Kevin T.,
Tseng YiHsiung,
Saier Milton H.
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10889.x
Subject(s) - phylogenetic tree , biology , genome , genetics , conserved sequence , protein family , phylogenetics , bacteria , membrane protein , protein superfamily , archaea , sequence alignment , computational biology , gene , peptide sequence , evolutionary biology , membrane
Mitochondrial Oxa1p homologs have been shown to function in protein export and membrane insertion in bacteria, mitochondria and chloroplasts, but their mode of action, organismal distribution and evolutionary origins are poorly understood. All sequenced homologs of Oxa1p were retrieved from the databases and multiply aligned. All organisms with a fully sequenced genome possess at least one Oxa1p homolog showing that the family is truly ubiquitous. Most prokaryotes possess just one Oxa1p homolog, but several Gram‐positive bacteria and one archaeon possess two, and eukaryotes may have as many as six. Although these proteins vary in length over a 5‐fold range, they exhibit a common hydrophobic core region of about 200 residues. Multiple sequence alignments reveal conserved residues and provide the basis for structural and phylogenetic analyses that serve to characterize the Oxa1 family.