Original language | English (US) |
---|---|
Pages (from-to) | 251-266 |
Number of pages | 16 |
Journal | Methods in enzymology |
Volume | 250 |
Issue number | C |
DOIs | |
State | Published - Jan 1 1995 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
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In: Methods in enzymology, Vol. 250, No. C, 01.01.1995, p. 251-266.
Research output: Contribution to journal › Article › peer-review
}
TY - JOUR
T1 - Yeast STE 14 methyltransferase, expressed as TrpE-STE 14 fusion protein in Escherichia coli, for in Vitro Carboxylmethylation of prenylated polypeptides
AU - Hrycyna, Christine A.
AU - Wait, Stephanie J.
AU - Backlund, Peter S.
AU - Michaelis, Susan
N1 - Funding Information: We are indebted to D. S. King for peptide synthesis, mass spectrometry, and unending technical support. We thank L. Wood and A. Moser (University of California, San Francisco) for rat tissues and R. Kim and S.-H. Kim for Xenopus oocyte samples and many helpful discussions. We also thank S. Rosenberg and C. C. Yang (Protos, Emeryville, CA) for dan-sylated peptides and members of the laboratory of J. R. for insightful discussions during the course of the experiments. The work was supported by the California Tobacco-Related Disease Research Program (2FT0030 to M. N. A. and IRT26 to J. R.) and by a National Institute of Environmental Health Sciences Mutagenesis Center grant (P30 ESO 1896). Funding Information: We thank Steve Clarke in whose laboratory part of this work was carried out (by C. A. H.) and Kathleen Green Vancura for technical assistance in construction of trpE-STE14 gene fusions. We also thank Carol Berkower for helpful comments on the manuscript. This work was supported by grants from the National Institutes of Health to Steve Clarke (GM26020) and to S. M. (GM41223). C. A. H. was supported in part by a U.S. Public Health Service Training Grant (GM07185).
PY - 1995/1/1
Y1 - 1995/1/1
UR - http://www.scopus.com/inward/record.url?scp=0029022640&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029022640&partnerID=8YFLogxK
U2 - 10.1016/0076-6879(95)50077-4
DO - 10.1016/0076-6879(95)50077-4
M3 - Article
C2 - 7651156
AN - SCOPUS:0029022640
SN - 0076-6879
VL - 250
SP - 251
EP - 266
JO - Methods in enzymology
JF - Methods in enzymology
IS - C
ER -