Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 3, Pages 1398-1410Publisher
ELSEVIER
DOI: 10.1074/jbc.M115.673491
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Funding
- Kentucky Science and Engineering Foundation [KSEF-2841-RDE-016]
- National Science Foundation [NSF-IIA-1355438, NSF-IOS-1456884]
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [1456884] Funding Source: National Science Foundation
- Office Of The Director
- Office of Integrative Activities [1355438] Funding Source: National Science Foundation
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Posttranslational lipid modifications mediate the membrane attachment of Rab GTPases, facilitating their function in regulating intracellular vesicular trafficking. In Arabidopsis, most Rab GTPases have two C-terminal cysteines and potentially can be double-geranylgeranylated by heterodimeric Rab geranylgeranyltransferases (Rab-GGTs). Genes encoding two putative alpha subunits and two putative beta subunits of Rab-GGTs have been annotated in the Arabidopsis thaliana genome, but little is known about Rab-GGT activity in Arabidopsis. In this study, we demonstrate that four different heterodimers can be formed between putative Arabidopsis Rab-GGT alpha subunits RGTA1/ RGTA2 and beta subunits RGTB1/RGTB2, but only RGTA1.RGTB1 and RGTA1.RGTB2 exhibit bona fide Rab-GGT activity, and they are biochemically redundant in vitro. We hypothesize that RGTA2 function might be disrupted by a 12-amino acid insertion in a conserved motif. We present evidence that Arabidopsis Rab-GGTs may have preference for prenylation of C-terminal cysteines in particular positions. We also demonstrate that Arabidopsis Rab-GGTs can not only prenylate a great variety of Rab GTPases in the presence of Rab escort protein but, unlike Rab-GGT in yeast and mammals, can also prenylate certain non-Rab GTPases independently of Rab escort protein. Our findings may help to explain some of the phenotypes of Arabidopsis protein prenyltransferase mutants.
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