ArticlePlant molecular biology1993
The disappearance of an hsc70 species in mung bean seed during germination: purification and characterization of the protein.
Article in Plant molecular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 18 citations in OpenAlex.
- Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family.Plant physiology · 2001Article
- Molecular chaperones and protein folding in plants.Plant molecular biology · 1996Review
- Binding of ATP and ATP analogues to the uncoating ATPase Hsc70 (70 kDa heat-shock cognate protein).The Biochemical journal · 1996Article
- Cytoplasmic HSP70 homologues of pea: differential expression in vegetative and embryonic organs.Plant molecular biology · 1995Article
- Isolation of a cDNA encoding a 70 kDa heat-shock cognate protein expressed in vegetative tissues of Arabidopsis thaliana.Plant molecular biology · 1994Article
- Expression of sunflower low-molecular-weight heat-shock proteins during embryogenesis and persistence after germination: localization and possible functional implications.Plant molecular biology · 1994Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have purified a 73 kDa protein from the cytosolic fraction of mung bean seeds. It comprises 0.5-1% of the total protein in seeds. This purified protein is a bona fide hsc70 on the basis of several lines of evidence. First, antibodies against bovine brain hsc70 cross-react with the purified 73 kDa protein. Second, the purified protein comigrates on two-dimensional gels with one of the heat-inducible hsc70s in mung bean seedlings. Third, similar to other hsc70 species, the purified 73 kDa protein has a high affinity for ATP. Finally, the hydrolysis of ATP by the purified protein can be stimulated by peptides; ATPase activity increases from 40 nmol/h to 165 nmol/h per mg of protein. The purified mung bean hsc70 autophosphorylates at a substoichiometric level. Moreover, the amount of this hsc70 species diminishes while new species of hsc70s appear after germination, suggesting that the expression of hsc70 in mung bean is subject to developmental regulation.
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