| Structural highlights
Function
[SR54C_ARATH] Involved in cotranslational and post-translational sorting of thylakoid proteins. Binds GTP specifically. Activates the GTPase activity of CPFTSY when bound together. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids.[1] [2] [3] [4] [CFTSY_ARATH] Signal recognition particle receptor protein. Binds GTP specifically. The GTPase activity is inhibited by the N-terminus of the protein until binding to the thylakoid membrane. Activates the GTPase activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for light-harvesting chlorophyll a/b-binding protein (LHCP) integration into thylakoids. Might be also functionally linked to the Sec translocation machinery.[5] [6] [7] [8] [9] [10]
Publication Abstract from PubMed
The signal recognition particle (SRP) is a ribonucleoprotein complex with a key role in targeting and insertion of membrane proteins. The two SRP GTPases, SRP54 (Ffh in bacteria) and FtsY (SRalpha in eukaryotes), form the core of the targeting complex (TC) regulating the SRP cycle. The architecture of the TC and its stimulation by RNA has been described for the bacterial SRP system while this information is lacking for other domains of life. Here, we present the crystal structures of the GTPase heterodimers of archaeal (Sulfolobus solfataricus), eukaryotic (Homo sapiens), and chloroplast (Arabidopsis thaliana) SRP systems. The comprehensive structural comparison combined with Brownian dynamics simulations of TC formation allows for the description of the general blueprint and of specific adaptations of the quasi-symmetric heterodimer. Our work defines conserved external nucleotide-binding sites for SRP GTPase activation by RNA. Structural analyses of the GDP-bound, post-hydrolysis states reveal a conserved, magnesium-sensitive switch within the I-box. Overall, we provide a general model for SRP cycle regulation by RNA.
Structural Basis for Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex.,Wild K, Bange G, Motiejunas D, Kribelbauer J, Hendricks A, Segnitz B, Wade RC, Sinning I J Mol Biol. 2016 May 27. pii: S0022-2836(16)30184-X. doi:, 10.1016/j.jmb.2016.05.015. PMID:27241309[11]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tu CJ, Schuenemann D, Hoffman NE. Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes. J Biol Chem. 1999 Sep 17;274(38):27219-24. PMID:10480939
- ↑ Groves MR, Mant A, Kuhn A, Koch J, Dubel S, Robinson C, Sinning I. Functional characterization of recombinant chloroplast signal recognition particle. J Biol Chem. 2001 Jul 27;276(30):27778-86. Epub 2001 May 16. PMID:11356852 doi:http://dx.doi.org/10.1074/jbc.M103470200
- ↑ Jaru-Ampornpan P, Chandrasekar S, Shan SO. Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA. Mol Biol Cell. 2007 Jul;18(7):2636-45. Epub 2007 May 2. PMID:17475780 doi:http://dx.doi.org/10.1091/mbc.E07-01-0037
- ↑ Rutschow H, Ytterberg AJ, Friso G, Nilsson R, van Wijk KJ. Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. Plant Physiol. 2008 Sep;148(1):156-75. doi: 10.1104/pp.108.124545. Epub 2008 Jul , 16. PMID:18633119 doi:http://dx.doi.org/10.1104/pp.108.124545
- ↑ Kogata N, Nishio K, Hirohashi T, Kikuchi S, Nakai M. Involvement of a chloroplast homologue of the signal recognition particle receptor protein, FtsY, in protein targeting to thylakoids. FEBS Lett. 1999 Mar 26;447(2-3):329-33. PMID:10214972
- ↑ Tu CJ, Schuenemann D, Hoffman NE. Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes. J Biol Chem. 1999 Sep 17;274(38):27219-24. PMID:10480939
- ↑ Yuan J, Kight A, Goforth RL, Moore M, Peterson EC, Sakon J, Henry R. ATP stimulates signal recognition particle (SRP)/FtsY-supported protein integration in chloroplasts. J Biol Chem. 2002 Aug 30;277(35):32400-4. Epub 2002 Jun 24. PMID:12105232 doi:http://dx.doi.org/10.1074/jbc.M206192200
- ↑ Jaru-Ampornpan P, Chandrasekar S, Shan SO. Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA. Mol Biol Cell. 2007 Jul;18(7):2636-45. Epub 2007 May 2. PMID:17475780 doi:http://dx.doi.org/10.1091/mbc.E07-01-0037
- ↑ Asakura Y, Kikuchi S, Nakai M. Non-identical contributions of two membrane-bound cpSRP components, cpFtsY and Alb3, to thylakoid biogenesis. Plant J. 2008 Dec;56(6):1007-17. doi: 10.1111/j.1365-313X.2008.03659.x. Epub 2008, Aug 21. PMID:18764927 doi:http://dx.doi.org/10.1111/j.1365-313X.2008.03659.x
- ↑ Marty NJ, Rajalingam D, Kight AD, Lewis NE, Fologea D, Kumar TK, Henry RL, Goforth RL. The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity. J Biol Chem. 2009 May 29;284(22):14891-903. doi: 10.1074/jbc.M900775200. Epub, 2009 Mar 17. PMID:19293157 doi:http://dx.doi.org/10.1074/jbc.M900775200
- ↑ Wild K, Bange G, Motiejunas D, Kribelbauer J, Hendricks A, Segnitz B, Wade RC, Sinning I. Structural Basis for Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex. J Mol Biol. 2016 May 27. pii: S0022-2836(16)30184-X. doi:, 10.1016/j.jmb.2016.05.015. PMID:27241309 doi:http://dx.doi.org/10.1016/j.jmb.2016.05.015
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