The Drosophila kinesin light chain: primary structure and interaction with kinesin heavy chain

Kinesin light chain (KLC) complexes with the kinesin heavy chain (KHC) to form native kinesin. Proposed functions of KLC include coupling of cargo to KHC or modulation of KHC ATPase activity. In this paper we use the KHC tail, which binds specifically to KLC in blot overlays, as a probe to clone a c...

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Bibliographic Details
Published in:The Journal of biological chemistry 1993-06, Vol.268 (18), p.13657-13666
Main Authors: Gauger, A.K, Goldstein, L.S.B
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biological and medical sciences
Blotting, Western
Cell structures and functions
CLONACION
CLONAGE
Cloning, Molecular
Cytoskeleton, cytoplasm. Intracellular movements
DNA
DROSOPHILA
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Kinesin - chemistry
Kinesin - genetics
Kinesin - metabolism
Molecular and cellular biology
Molecular Sequence Data
Protein Conformation
PROTEINAS
PROTEINE
Rats
Recombinant Fusion Proteins - metabolism
RNA, Messenger - metabolism
Sequence Homology, Amino Acid
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Summary:Kinesin light chain (KLC) complexes with the kinesin heavy chain (KHC) to form native kinesin. Proposed functions of KLC include coupling of cargo to KHC or modulation of KHC ATPase activity. In this paper we use the KHC tail, which binds specifically to KLC in blot overlays, as a probe to clone a cDNA encoding KLC from a Drosophila expression library. The identified clone encodes a protein with 70% amino acid identity to rat KLC. Drosophila KLC is predicted to form an alpha-helical coiled-coil between residues 34 and 129, followed by five imperfect tandem repeats of unknown function and a sixth shorter motif. These repeats are highly conserved across species. The Drosophila KLC gene is located at 69D on the third chromosome and is widely expressed, with 1.8-kb transcripts in most tissues, and slightly smaller transcripts in gonads. Finally, we present evidence that the heptad repeats of KLC are required for interaction with the KHC tail. Since the KHC tail used in our assay includes about 20 heptad repeats, this result suggests that KHC and KLC interact via coiled-coils. Such an interaction could provide stability to the KHC-KLC complex in vivo
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)38698-3