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Cited by 43Microtubule and mitosis dynamicsGenetic and Kidney Cyst DiseasesATP Synthase and ATPases Research

The DOI matches its Crossref record.

A latent activity dynein-like cytoplasmic magnesium adenosine triphosphatase.

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Asai, D J, Wilson, L·1985·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(20)71152-x
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Abstract

A MgATPase has been isolated and characterized from unfertilized sea urchin eggs which is very similar, but not identical, to latent activity axonemal dynein. The cytoplasmic MgATPase activity sediments at 20 S, slightly slower than 21 S latent activity flagellar dynein. Activity is stimulated by nonionic detergent and is inhibited by sodium orthovanadate but is not as sensitive to vanadate as is 21 S flagellar dynein. The egg 20 S MgATPase is composed, at least in part, of three high molecular weight polypeptides. In addition, two intermediate-sized polypeptides appear to co-sediment with the 20 S MgATPase activity. A novel microtubule-affinity assay reveals that high molecular weight polypeptides 1 and 2 of the egg 20 S MgATPase can bind to reassembled microtubules and can be released from the microtubules with MgATP2-. Further, the apparent specific activity of the egg MgATPase is enriched 15-fold by a single microtubule binding step. The results suggest that the cytoplasmic 20 S MgATPase is a dynein-like microtubule translocator which resides in the unfertilized egg awaiting future incorporation onto microtubules in order to perform work. The egg 20 S enzyme might function in cytoplasmic microtubule-mediated movement or it might be a precursor of embryonic ciliary dynein.

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Research works printed but not linked: 24

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Metadata

Authors
Asai, D. J., & Wilson, L.
Affiliations
University of California, Santa Barbara (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1985-01
Volume
260
Issue
2
Pages
699-702
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(20)71152-x
OpenAlex
W1604973744
Cited by
43
References
0
Citations by year
2025: 1 · 2018: 1 · 2017: 1
FWCI
4.41
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institute of Neurological Disorders and Stroke (NS 13560)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD16956)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords
sea urchin eggs, axonemal dynein, flagellar dynein, microtubule binding, microtubule translocation, polypeptide composition
MeSH terms
Adenosine Triphosphatases, Animals, Centrifugation, Density Gradient, Dyneins, Electrophoresis, Polyacrylamide Gel, Female, Microtubules, Molecular Weight, Oocytes, Sea Urchins, Ca(2+) Mg(2+)-ATPase

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CoChat. (2026). Citation check: A latent activity dynein-like cytoplasmic magnesium adenosine triphosphatase. https://app.cochat.ai/papers/10.1016/s0021-9258(20)71152-x
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Asai, D. J., & Wilson, L. (1985). A latent activity dynein-like cytoplasmic magnesium adenosine triphosphatase. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(20)71152-x