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Literature summary for 3.6.5.4 extracted from

  • Nguyen, T.X.; Chandrasekar, S.; Neher, S.; Walter, P.; Shan, S.O.
    Concerted complex assembly and GTPase activation in the chloroplast signal recognition particle (2011), Biochemistry, 50, 7208-7217.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant cpSRP54 in Escherichia coli strain Rosetta BL21 Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
A142W site-directed mutagenesis, the mutant cpSRP54 exhibits the same GTP-dependent complex assembly kinetics as wild-type cpSRP54 Arabidopsis thaliana
A143L site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview Arabidopsis thaliana
A143W site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview Arabidopsis thaliana
A168W site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview Arabidopsis thaliana
A169L site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview Arabidopsis thaliana
A169W site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview Arabidopsis thaliana
D137A site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview Arabidopsis thaliana
D163A site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview Arabidopsis thaliana
additional information binding kinetics and competing inhibitions with several bacterial cpFtsY mutants, affinities of mutant bacterial cpFtsYs for cpSRP54, and complex formations, overview Arabidopsis thaliana
R140A site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview Arabidopsis thaliana
R166A site-directed mutagenesis, mutant cpSRP54 GTP-dependent complex assembly kinetics compared to the wild-type cpSRP54, overview Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast chloroplast SRP Arabidopsis thaliana 9507
-
cytosol cytosolic SRP Arabidopsis thaliana 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Arabidopsis thaliana
-
GDP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
gene cpSRP54
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant cpSRP54 from Escherichia coli strain Rosetta BL21 by two steps of cation exchange chromatography Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
Arabidopsis thaliana GDP + phosphate
-
?

Subunits

Subunits Comment Organism
More homology modeling and structure analysis, overview Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
cpSRP54
-
Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Arabidopsis thaliana

General Information

General Information Comment Organism
additional information concerted complex assembly and GTPase activation occurs in the chloroplast signal recognition particle. In contrast to the cytosolic homologues, GTPase activation in the chloroplast SRP-SR complex contributes marginally to the targeting of LHC proteins. Complex assembly and GTPase activation are highly coupled in the chloroplast SRP and SR and suggest that the chloroplast GTPases may forego the GTPase activation step as a key regulatory point. Homology model of the cpSRP54·cpFtsY complex based on superposition of the crystal structure of apo-cpFtsY onto that of Thermus aquaticus SR, i.e. FtsY, in complex with Ffh. Thermodynamic and kinetics for formation of the cpSRP54-cpFtsY complex, formed by wild-types and mutants, detailed overview. IBD loops play essential roles in both complex assembly and GTPase activation Arabidopsis thaliana
physiological function the universally conserved signal recognition particle, SRP, and SRP receptor, SR, mediate the cotranslational targeting of proteins to cellular membranes. In contrast, a unique chloroplast SRP in green plants is primarily dedicated to the post-translational targeting of light harvesting chlorophyll a/b binding proteins. In both pathways, dimerization and activation between the SRP and SR GTPases mediate the delivery of cargo. Efficient assembly of the cpSRP54-cpFtsY complex is crucial for the targeting and integration of LHCP, whereas GTPase activation and/or GTP hydrolysis plays a modulatory role to help enhance the efficiency of targeting Arabidopsis thaliana