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Rearranging the Domains of Pepsinogen by Xinli Lin; Gerald Koelsch; Jeffrey A. Loy; Jordan Tang is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Most eukaryotic aspartic protease zymogens are synthesized as a single polypeptide chain that contains two distinct homologous lobes and a __pro__ peptide, which is removed upon activation. In pepsinogen, the __pro__ peptide precedes the N‐terminal lobe (designated __pep__) and the C‐terminal lobe (designated __sin__). Based on the three‐dimensional structure of pepsinogen, we have designed a pepsinogen polypeptide with the internal rearrangement of domains from __pro‐pep‐sin__ (native pepsinogen) to __sin‐pro‐pep__. The domain‐rearranged zymogen also contains a 10‐residue linker designed to connect __sin__ and __pro__ domains. Recombinant __sin‐pro‐pep__ was synthesized in __Escherichia coli__, refolded from 8 M urea, and purified. Upon acidification, __sin‐pro‐pep__ autoactivates to a two‐chain enzyme. However, the emergence of activity is much slower than the conversion of the single‐chain zymogen to a two‐chain intermediate. In the activation of native pepsinogen and __sin‐pro‐pep__, the __pro__ region is cleaved at two sites between residues 16P and 17P and 44P and 1 successively, and complete activation of __sin‐pro‐pep__ requires an additional cleavage at a third

Who reads Rearranging the Domains of Pepsinogen?

Author

Xinli Lin; Gerald Koelsch; Jeffrey A. Loy; Jordan Tang

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

1995

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)