Reference - Detail
|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.|
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.
|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*|
|WOS Category||BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY|
|Arabidopsis / Cultured plant cells, genes||pdp|