Sequences of sea urchin kinesin light chain isoforms

Karen P. Wedaman, Alex E. Knight, John Kendrick-Jones, Jonathan M. Scholey

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)155-158
Number of pages4
JournalJournal of Molecular Biology
Volume231
Issue number1
StatePublished - 1993

Keywords

  • Kinesin
  • Light chain sequences
  • Organelle transport

ASJC Scopus subject areas

  • Virology

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