Abstract
Most eukaryotic proteins are post-translationally modified, and modification has profound effects on protein function. One key modification is the attachment of a lipid group to certain amino acids; this typically facilitates subcellular targeting (association with a membrane) and protein–protein interactions (by virtue of the large hydrophobic moiety). Most widely recognized are lipid modifications of proteins involved in developmental signaling, but proteins with structural roles are also lipid-modified. The three known types of intracellular protein lipid modifications are S-acylation, N-myristoylation, and prenylation. In plants, genetic analysis of the enzymes involved, along with molecular analysis of select target proteins, has recently shed light on the roles of lipid modification in key developmental processes, such as meristem function, flower development, polar cell elongation, cell differentiation, and hormone responses. In addition, while lipid post-translational mechanisms are generally conserved among eukaryotes, plants differ in the nature and function of target proteins, the effects of lipid modification on target proteins, and the roles of lipid modification in developmental processes.
Highlights
With the rapid advancement of genome sequencing technologies, it is possible to know virtually all the genes, and the full complement of proteins, in an increasing number of organisms
Hundreds of proteins are known or thought to be lipid modified in plants; this review focuses on the role of protein lipid modifications in developmental signaling and plant growth processes
In vitro studies show that Arabidopsis protein farnesyltransferase (PFT) has nearly as high affinity for leucine as it does for the standard alanine, cysteine, glutamine, methionine, and serine in the X position of the CaaX target sequence, while protein geranylgeranyltransferase-I (PGGT) shows weak but measurable affinity for non-leucine terminal amino acids (Andrews et al, 2010), which helps explain both the weak era1 and very weak ggb mutant phenotypes compared to plp
Summary
With the rapid advancement of genome sequencing technologies, it is possible to know virtually all the genes, and the full complement of proteins, in an increasing number of organisms. Mutations in the Arabidopsis α subunit shared between PFT and PGGT, termed PLURIPETALA (PLP), cause severe developmental phenotypes, including much larger shoot meristems, stem fasciation, and extra floral organs (Running et al, 2004). In vitro studies show that Arabidopsis PFT has nearly as high affinity for leucine as it does for the standard alanine, cysteine, glutamine, methionine, and serine in the X position of the CaaX target sequence, while PGGT shows weak but measurable affinity for non-leucine terminal amino acids (Andrews et al, 2010), which helps explain both the weak era and very weak ggb mutant phenotypes compared to plp.
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