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Title: ENLARGED MERISTEMS AND DELAYED GROWTH IN PLP MUTANTS RESULT FROM LACK OF CAAX PRENYLTRANSFERASES.

Author
item RUNNING, MARK - UCB-ARS PLNT GENE EXP CTR
item LAVY, M - UCB PLNT & MICROBIAL BIOL
item STERNBERG, H - UCB PLNT & MICROBIAL BIOL
item GALICHET, A - UCB PLNT & MICROBIAL BIOL
item GRUISSEM, WILLIAM - UCB PLNT & MICROBIAL BIOL
item HAKE, SARAH - UCB-ARS PLNT GENE EXP CTR
item ORI, NAOMI - UCB-ARS PLNT GENE EXP CTR
item YALOVSKY, S - UCB PLNT & MICROBIAL BIOL

Submitted to: Proceedings of the National Academy of Sciences (PNAS)
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/1/2004
Publication Date: 5/18/2004
Citation: Running, M.P., Lavy, M., Sternberg, H., Galichet, A., Gruissem, W., Hake, S., Ori, N., Yalovsky, S. 2004. Enlarged meristems and delayed growth in plp mutants result from lack of CaaX prenyltransferases. Proceedings of the National Academy of Sciences USA 101(20):7815-20.

Interpretive Summary: Meristems require a myriad of intercellular signaling pathways for coordination of cell division within and between functional zones and clonal cell layers. This control of cell division ensures a constant availability of stem cells throughout the life span of the meristem while limiting overproliferation of meristematic cells and maintaining the meristem structure. We identified pluripetala (plp) mutants based on their dramatically larger meristems and increased floral organ number.

Technical Abstract: We have undertaken a genetic screen to identify additional components of meristem signaling pathways. PLURIPETALA encodes the alpha-subunit shared between protein farnesyltransferase and protein geranylgeranyltransferase-I. plp mutants also have altered abscisic acid responses and overall much slower growth rate. plp is epistatic to mutations in the beta-subunit of farnesyltransferase and shows a synergistic interaction with clavata3 mutants. plp mutants lead to insights into the mechanism of meristem homeostasis and provide a unique in vivo system for studying the functional role of prenylation in eukaryotes.