Peptide Binding and Release by Proteins Implicated as Catalysts of Protein Assembly

American Association for the Advancement of Science (AAAS) - Tập 245 Số 4916 - Trang 385-390 - 1989
Gregory C. Flynn1, Thomas G. Chappell2, James E. Rothman1
1Department of Biology, Lewis Thomas Laboratory, Princeton University, NJ 08544.
2Imperial Cancer Research Fund, WC2A 3PX London, England.

Tóm tắt

Two members of the hsp70 family, termed hsc70 and BiP, have been implicated in promoting protein folding and assembly processes in the cytoplasm and the lumen of the endoplasmic reticulum, respectively. Short hydrophilic (8 to 25 residues) synthetic peptides have now been tested as possible mimics of polypeptide chain substrates to help define an enzymatic basis for these activities. Both BiP and hsc70 have specific peptide binding sites. Peptide binding elicits hydrolysis of adenosine triphosphate, with the subsequent release of bound peptide.

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Tài liệu tham khảo

10.1126/science.181.4096.223

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American Association for the Advancement of Science (AAAS)

Tập 245 Số 4916

385-390

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