We isolated a cDNA clone from Arabidopsis thaliana encoding the TCA cycle enzyme, citrate synthase. The plant enzyme displays 48 ~o and 44~o amino acid residue similarity with the pig, and yeast polypeptides, respectively. Many proteins, including citrate synthase, which are destined to reside in or
Characterisation of PHSP1, a cDNA encoding a mitochondrial HSP70 fromPisum sativum
โ Scribed by Felicity Z. Watts; Andrew J. Walters; Anthony L. Moore
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 898 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0167-4412
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โฆ Synopsis
A pea cDNA clone, PHSP1, encoding a member of the HSP70 gene family has been isolated. DNA sequence analysis indicates that the protein encoded by PHSP1 is a homologue of the mitochondrial HSP70 proteins, SSP1 from Schizosaccharomyces pombe and SSC1 from S. cerevisiae. It contains an amino-terminal extension of 50 amino acids, rich in basic and hydroxyl amino acids, similar to other plant mitochondrial leader sequences. Western blot analysis indicates that the PHSP1 protein is associated only with mitochondria and not with any other sub-cellular organelle or cytoplasm. Further confirmation of its location within mitochondria was obtained from in vitro protein translocation experiments into purified Pisum sativum mitochondria. It was observed that the precursor protein was efficiently imported and that it is processed to produce a protein with an Mr of the anticipated size of the mature protein. Results are discussed with respect to the structure and function of the mitochondrial HSP70 protein.
๐ SIMILAR VOLUMES
Chaperonin (Cpn) is one of the molecular chaperones. Cpn10 is a co-factor of Cpn60, which regulates Cpn60-mediated protein folding. It is known that Cpn10 is located in mitochondria and chloroplasts in plant cells. The Escherichia coli homologue of Cpn10 is called GroES. A cDNA for the Cpn10 homolog