Kinesin light chain in a eubacterium.
A eubacterial homolog of a kinesin light chain gene has been isolated and characterized from the cyanobacterium Plectonema boryanum. Although the eubacterial and eukaryotic kinesin light chains are highly similar in amino acid sequence, the eubacterial sequence differs in several distinguishing structural features, including the absence of a putative PEST domain and the presence of additional highly conserved imperfect tandem repeats. Two soluble kinesin light chain antigens have been identified from whole-cell lysates by immunoblot analysis. Attempts to identify a canonical kinesin heavy-chain gene or protein were unsuccessful, suggesting that a kinesin heavy chain may be absent or unnecessary for kinesin light-chain function in this eubacterium. Our findings establish that certain basal elements of eukaryotic cellular transport appear to be resident in eubacteria. We discuss the possibility that the eukaryotic kinesin light chain was acquired by lateral gene transfer.
Celerin
M
M
University of Western Ontario, Department of Plant Sciences, London, Canada. mcelerin@sunflower.bio.indiana.edu
Gilpin
A A
AA
Dossantos
G
G
Laudenbach
D E
DE
Clarke
M W
MW
Beushausen
S
S
D000595:Amino Acid Sequence; D015153:Blotting, Western; D003001:Cloning, Molecular; D000458:Cyanobacteria / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D016547:Kinesins; D008869:Microtubule-Associated Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D008869:Microtubule-Associated Proteins; D016547:Kinesins