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Cited by 37Microtubule and mitosis dynamicsProtein Structure and DynamicsGenomics and Chromatin Dynamics

Light chains of sea urchin kinesin identified by immunoadsorption

Johnson, Catharine S., Buster, Dan, Scholey, Jonathan M.·1990·Cell Motility
DOI 10.1002/cm.970160307
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Abstract

Previous studies with monoclonal antibodies indicate that sea urchin kinesin contains two heavy chains arranged in parallel such that their N-terminal ends fold into globular mechanochemical heads attached to a thin stalk ending in a bipartite tail [Scholey et al., 1989]. In the present, complementary study, we have used the monoclonal antikinesin, SUK4, to probe the quaternary structure of sea urchin (Strongylocentrotus purpuratus) kinesin. Kinesin prepared from sea urchin cytosol sedimented at 9.6 S on sucrose density gradients and consisted of 130-kd heavy chains plus an 84-kd/78 kd doublet (1 mol heavy chain: 1 mol doublet determined by gel densitometry). Low levels of 110-kd and 90-kd polypeptides were sometimes present as well. The 84-kd/78 kd polypeptides are thought to be light chains because they were precipitated from the kinesin preparation at a stoichiometry of one mol doublet per 1 mol heavy chain using SUK4-Sepharose immunoaffinity resins. The 110-kd and 90-kd peptides, by contrast, were removed using this immunoadsorption method. SUK4-Sepharose immunoaffinity chromatography was also used to purify the 130-kd heavy chain and 84-kd/78-kd doublet (1 mol heavy chain: 1 mol doublet) directly from sea urchin egg cytosolic extracts, and from a MAP (microtubule-associated protein) fraction eluted by ATP from microtubules prepared in the presence of AMPPNP but not from microtubules prepared in ATP. The finding that sea urchin kinesin contains equimolar quantities of heavy and light chains, together with the aforementioned data on kinesin morphology, suggests that native sea urchin kinesin is a tetramer assembled from two light chains and two heavy chains.

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  • Conventional kinesin, kinesin-I, is a heterotetramer of two KHC subunits and two KLC subunits in a 1:1 stoichiometric ratio.

    “Conventional kinesin, kinesin-I, is a heterotetramer of two kinesin heavy chain (KHC) subunits (KIF5A, KIF5B, or KIF5C) and two kinesin light chain (KLC) subunits.”

    From Defective kinesin heavy chain behavior in mouse kinesin light chain mutants (1999) · cites this paper as Johnson et al. 1990

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Authors
Johnson, C. S., Buster, D., & Scholey, J. M.
Affiliations
University of California, Davis (US)
Corresponding author
Scholey, Jonathan M.
Venue
Cell Motility
Publisher
Wiley
Published
1990-01
Volume
16
Issue
3
Pages
204-213
ISSN
0886-1544 (ISSN-L)
DOI
10.1002/cm.970160307
OpenAlex
W1998611859
Cited by
37
References
35
Citations by year
2025: 1 · 2018: 1 · 2016: 1 · 2015: 1
FWCI
1.73
Type
journal article
Language
en
Open access
closed
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 5513 d)
Locations
  • Cell Motility and the Cytoskeleton (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • American Cancer Society
  • March of Dimes Foundation
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords
Strongylocentrotus purpuratus, kinesin light chain, kinesin heavy chain, immunoaffinity chromatography, microtubule-associated proteins, microtubule binding
MeSH terms
Adenosine Triphosphatases, Animals, Antibodies, Monoclonal, Chromatography, Affinity, Immunosorbent Techniques, Microtubule Proteins, Molecular Weight, Oocytes, Sea Urchins, Kinesins, Macromolecular Substances

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