Email updates

Keep up to date with the latest news and content from BMC Evolutionary Biology and BioMed Central.

Open Access Research article

Multiple domain insertions and losses in the evolution of the Rab prenylation complex

Rita Rasteiro and Jose B Pereira-Leal*

Author Affiliations

Instituto Gulbenkian de Ciência, Apartado 14, P-2781-901 Oeiras Portugal

For all author emails, please log on.

BMC Evolutionary Biology 2007, 7:140  doi:10.1186/1471-2148-7-140

Published: 17 August 2007



Rab proteins are regulators of vesicular trafficking, requiring a lipid modification for proper function, prenylation of C-terminal cysteines. This is catalysed by a complex of a catalytic heterodimer (Rab Geranylgeranyl Transferase – RabGGTase) and an accessory protein (Rab Escort Protein. REP). Components of this complex display domain insertions relative to paralogous proteins. The function of these inserted domains is unclear.


We profiled the domain architecture of the components of the Rab prenylation complex in evolution. We identified the orthologues of the components of the Rab prenylation machinery in 43 organisms, representing the crown eukaryotic groups. We characterize in detail the domain structure of all these components and the phylogenetic relationships between the individual domains.


We found different domain insertions in different taxa, in α-subunits of RGGTase and REP. Our results suggest that there were multiple insertions, expansions and contractions in the evolution of this prenylation complex.