Functional analysis of isolated cpn10 domains and conserved amino acid residues in spinach chloroplast co-chaperonin by site-directed mutagenesis
Author:
Publisher
Springer Science and Business Media LLC
Subject
Plant Science,Genetics,Agronomy and Crop Science,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/BF00014976.pdf
Reference34 articles.
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2. Baneyx F, Gatenby AA: A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides. J Biol Chem 267: 11637?11644 (1992).
3. Barraclough R, Ellis RJ: Protein synthesis in chloroplasts, IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts. Biochim Biophys Acta 608: 19?31 (1980).
4. Bertsch U, Soll J, Seetharam R, Viitanen PV: Identification, characterization, and DNA sequence of a functional ?double? groES-like chaperonin from chloroplasts of higher plants. Proc Natl Acad Sci USA 89: 8696?8700 (1992).
5. Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB: The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature 371: 578?586 (1994).
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