RRC ID 4021
Author Richter CV, Träger C, Schünemann D.
Title Evolutionary substitution of two amino acids in chloroplast SRP54 of higher plants cause its inability to bind SRP RNA.
Journal FEBS Lett
Abstract The chloroplast signal recognition particle (cpSRP) consists of a conserved 54 kDa subunit (cpSRP54) and a unique 43 kDa subunit (cpSRP43) but lacks SRP-RNA, an essential and universally conserved component of cytosolic SRPs. High sequence similarity exists between cpSRP54 and bacterial SRP54 except for a plant-specific C-terminal extension containing the cpSRP43-binding motif. We found that cpSRP54 of higher plants lacks the ability to bind SRP-RNA because of two amino acid substitutions within a region corresponding to the RNA binding domain of cytosolic SRP54, whereas the C-terminal extension does not affect RNA binding. Phylogenetic analysis revealed that these mutations occur in the cpSRP54 homologues of higher plants but not in most algae.
Volume 582(21-22)
Pages 3223-9
Published 2008-9-22
DOI 10.1016/j.febslet.2008.08.014
PII S0014-5793(08)00696-0
PMID 18755190
MeSH Algal Proteins / genetics Algal Proteins / metabolism Amino Acid Motifs Amino Acid Substitution* Arabidopsis Proteins / classification Arabidopsis Proteins / genetics Arabidopsis Proteins / metabolism* Bacterial Proteins / genetics Bacterial Proteins / metabolism Binding Sites / genetics Chloroplast Proteins Conserved Sequence Evolution, Molecular* GTP-Binding Proteins / classification GTP-Binding Proteins / genetics GTP-Binding Proteins / metabolism* Molecular Sequence Data Mutation RNA, Bacterial / metabolism RNA, Chloroplast / metabolism Signal Recognition Particle / metabolism*
IF 3.057
Times Cited 17
Arabidopsis / Cultured plant cells, genes pdp