Sequences of sea urchin kinesin light chain isoforms.
We have deduced the amino acid sequences of four sea urchin (Strongylocentrotus purpuratus; SP) kinesin light chain (KLC) isoforms (SPKLC 1-4) and compared them to rat brain light chain sequences. Examination of the SPKLC open reading frames (SPKLC1, 649; SPKLC2, 677; SPKLC3, 686; and SPKLC4, 451 amino acid residues) reveals that the first 500 or so residues of the KLCs are highly conserved but the C-terminal ends of rat and sea urchin light chains are divergent; SPKLCs 1, 2 and 3 share a highly basic, 86 residue C-terminal segment that is missing from the shorter rat light chains and SPKLC4. The insertion of 28 and 37 residue segments at residue 563 of SPKLCs 2 and 3, respectively, gives rise to sequence heterogeneity at the C-terminal ends of the sea urchin KLCs. C-terminal sequence differences between light chains may provide inter- and intraspecies differences in the functional properties of the presumptive cargo attachment elements of kinesin.
Wedaman
K P
KP
Division of Biological Sciences, University of California, Davis 95616.
Knight
A E
AE
Kendrick-Jones
J
J
Scholey
J M
JM
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology; D016547:Kinesins / Q000235:genetics*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D017433:Protein Structure, Secondary; D051381:Rats; D012617:Sea Urchins / Q000201:enzymology* / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D046911:Macromolecular Substances; D016547:Kinesins