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The purification of M13 procoat, a membrane protein precursor.
Author(s) -
Zwizinski C.,
Wickner W.
Publication year - 1982
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1982.tb01210.x
Subject(s) - biology , membrane protein , membrane , biophysics , computational biology , microbiology and biotechnology , biochemistry
Many membrane proteins and most secreted proteins are initially made as precursors with an N‐terminal leader sequence. We now report the isolation of M13 procoat, the precursor of the membrane‐bound form of M13 coat protein. There are 40 000 copies of M13 procoat protein/cell during M13 amber 7 virus infection. Purified procoat is quantitatively cleaved by isolated leader peptidase to yield mature‐length coat protein. Rabbit antibodies to M13 procoat will precipitate procoat but not coat, suggesting that the antibody molecules are specifically recognizing the leader sequence or the conformation which it induces in the whole procoat molecule.