Protein prenylation in plants: old friends and new targets

Protein prenylation in plants: old friends and new targets Plant Molecular Biology 39: 865–870, 1999. © 1999 Kluwer Academic Publishers. Printed in the Netherlands. Mini-review ´ ´ Manuel Rodrıguez-Concepcion, Shaul Yalovsky and Wilhelm Gruissem Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkely, CA 94720, USA ( author for correspondence) Received 6 November 1998; accepted in revised form 19 November 1998 Introduction Proteins are modified by three types of prenyltransferases Protein prenylation is a post-translational protein Three different prenyltransferases catalyze protein modification that involves the formation of covalent prenylation reactions: a single farnesyl transferase thioether bonds between cysteines near the C-termini (FTase) and two geranylgeranyl transferases (GGTase- of target proteins and isoprenoid pathway interme- I and -II). Genetic analysis in yeast and biochemical diates 15-carbon farnesyldiphosphate (FPP) or 20- carbon geranylgeranyldiphosphate (GGPP). Protein studies in animals revealed that FTase and GGTase- prenylation was first discovered two decades ago as I are heterodimeric enzymes which share a com- a lipid modification of mating factors in fungi [10]. mon subunit but have distinc subunits that de- Later reports that all Ras proteins are prenylated [8] termine substrate specificity [21, 29]. Both FTase attracted much interest to protein prenylation in both and GGTase-I require zinc for catalytic http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Protein prenylation in plants: old friends and new targets

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Publisher
Springer Journals
Copyright
Copyright © 1999 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1006170020836
Publisher site
See Article on Publisher Site

Abstract

Plant Molecular Biology 39: 865–870, 1999. © 1999 Kluwer Academic Publishers. Printed in the Netherlands. Mini-review ´ ´ Manuel Rodrıguez-Concepcion, Shaul Yalovsky and Wilhelm Gruissem Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkely, CA 94720, USA ( author for correspondence) Received 6 November 1998; accepted in revised form 19 November 1998 Introduction Proteins are modified by three types of prenyltransferases Protein prenylation is a post-translational protein Three different prenyltransferases catalyze protein modification that involves the formation of covalent prenylation reactions: a single farnesyl transferase thioether bonds between cysteines near the C-termini (FTase) and two geranylgeranyl transferases (GGTase- of target proteins and isoprenoid pathway interme- I and -II). Genetic analysis in yeast and biochemical diates 15-carbon farnesyldiphosphate (FPP) or 20- carbon geranylgeranyldiphosphate (GGPP). Protein studies in animals revealed that FTase and GGTase- prenylation was first discovered two decades ago as I are heterodimeric enzymes which share a com- a lipid modification of mating factors in fungi [10]. mon subunit but have distinc subunits that de- Later reports that all Ras proteins are prenylated [8] termine substrate specificity [21, 29]. Both FTase attracted much interest to protein prenylation in both and GGTase-I require zinc for catalytic

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 19, 2004

References

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