Evolutionary substitution of two amino acids in chloroplast SRP54 of higher plants cause its inability to bind SRP RNA.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Richter CV,Träger C,Schünemann D

doi

10.1016/j.febslet.2008.08.014

subject

Has Abstract

pub_date

2008-09-22 00:00:00

pages

3223-9

issue

21-22

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(08)00696-0

journal_volume

582

pub_type

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