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Bos1p, a membrane protein required for ER to Golgi transport in yeast, co‐purifies with the carrier vesicles and with Bet1p and the ER membrane.
Author(s) -
Newman A.P.,
Groesch M.E.,
FerroNovick S.
Publication year - 1992
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.1460-2075.1992.tb05445.x
Subject(s) - biology , vesicle , golgi apparatus , transport protein , copi , microbiology and biotechnology , membrane , membrane transport protein , yeast , membrane transport , membrane protein , vesicular transport proteins , saccharomyces cerevisiae , biophysics , biochemistry , endoplasmic reticulum , secretory pathway , vacuolar protein sorting
BOS1 and BET1 are required for transport from the ER to the Golgi complex in yeast and genetically interact with each other and a subset of the other genes, whose products function at this stage of the secretory pathway. In a previous study, we reported that BOS1 encodes a putative 27 kDa membrane protein. Here we show that BET1 is structurally similar to the synaptobrevins and identical to the SLY12 gene product. Overexpression of SLY12 compensates for the loss of function of the ras‐like GTP‐binding protein Ypt1. Both Bos1p and Bet1p are cytoplasmically oriented membrane proteins. Bos1p co‐purifies with the ER to Golgi transport vesicles and co‐fractionates with Bet1p and the ER membrane.