Bet2p and Mad2p are components of a prenyltransferase that adds geranylgeranyl onto Ypt1p and Sec4p View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-11

AUTHORS

Yu Jiang, Guendalina Rossi, Susan Ferro-Novick

ABSTRACT

THREE different prenyltransferases have been identified in yeast and higher cells1–6, the farnesyltransferase and the type I and type II geranylgeranyltransferases (GGTase). The farnesyltransferase and GGTase-I modify peptides in vitro with the CAAX (C, Cys; A, aliphatic residue; X, terminal amino acid) consensus motif2,7. These enzymes are heterodimers that have different β-subunits and a shared α-subunit8. In yeast, the RAM2 gene encodes this α-subunit9. RAM2 is also homologous to MAD2, a yeast gene whose product has been implicated in the feedback control of mitosis10,11. We have shown that Bet2p is a component of the yeast GGTase-II (refs 6,12) that geranylgeranylates Yptlp, a small GTP-binding protein that mediates transport from the endoplasmic reticulum to the Golgi complex13–15. Here we report that Mad2p is a component of this enzyme. Bet2p forms a complex with Mad2p that appears to bind geranylgeranyl pyrophosphate, but not farnesyl pyrophosphate. The efficient transfer of geranylgeranyl onto small GTP-binding proteins requires the presence of an additional activity. More... »

PAGES

84-86

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/366084a0

DOI

http://dx.doi.org/10.1038/366084a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1047612664

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8232542


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