Protein Information

ID 4234
Name geranylgeranyltransferase (protein family or complex)
Synonyms Geranylgeranyl transferase; Geranylgeranyl transferases; RAB geranylgeranyltransferase; RAB geranylgeranyltransferases; geranyl geranyltransferase; geranyl geranyltransferases; geranylgeranyltransferase; geranylgeranyltransferases

Compound Information

ID 1715
Name abscisic acid
CAS

Reference

PubMed Abstract RScore(About this table)
15128936 Running MP, Lavy M, Sternberg H, Galichet A, Gruissem W, Hake S, Ori N, Yalovsky S: Enlarged meristems and delayed growth in plp mutants result from lack of CaaX prenyltransferases. Proc Natl Acad Sci U S A. 2004 May 18;101(20):7815-20. Epub 2004 May 5.
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 have undertaken a genetic screen to identify additional components of meristem signaling pathways. We identified pluripetala (plp) mutants based on their dramatically larger meristems and increased floral organ number. 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.
31(0,1,1,1)