%0 Journal Article %1 Goforth2004 %A Goforth, R. L. %A Peterson, E. C. %A Yuan, J. %A Moore, M. J. %A Kight, A. D. %A Lohse, M. B. %A Sakon, J. %A Henry, R. L. %D 2004 %J J Biol Chem %K Acid Amino Ankyrins/chemistry Apoproteins/chemistry Arabidopsis Biological Biosynthesis Chloroplasts/chemistry/metabolism Cloning, Complex/chemistry Data Deletion Electrophoresis, Endoplasmic Fusion GTP Gel Gene Glutathione Hydrolysis II Models, Molecular Particle/chemistry/*physiology Peptides/chemistry Phosphohydrolases/*chemistry Photosystem Plant Polyacrylamide Post-Translational Processing, Protein Proteins/chemistry Recognition Recombinant Reticulum/metabolism Ribosomes/chemistry Sequence Signal Structure, System Techniques Tertiary Thylakoids/metabolism Transduction Transferase/metabolism Transport Two-Hybrid %N 41 %P 43077-84 %T Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43 %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15292240 %V 279 %X The chloroplast signal recognition particle consists of a conserved 54-kDa GTPase and a novel 43-kDa chromodomain protein (cpSRP43) that together bind light-harvesting chlorophyll a/b-binding protein (LHCP) to form a soluble targeting complex that is subsequently directed to the thylakoid membrane. Homology-based modeling of cpSRP43 indicates the presence of two previously identified chromodomains along with a third N-terminal chromodomain. Chromodomain deletion constructs were used to examine the role of each chromodomain in mediating distinct steps in the LHCP localization mechanism. The C-terminal chromodomain is completely dispensable for LHCP targeting/integration in vitro. The central chromodomain is essential for both targeting complex formation and integration because of its role in binding the M domain of cpSRP54. The N-terminal chromodomain (CD1) is unnecessary for targeting complex formation but is required for integration. This correlates with the ability of CD1 along with the ankyrin repeat region of cpSRP43 to regulate the GTPase cycle of the cpSRP-receptor complex.

@article{Goforth2004, abstract = {The chloroplast signal recognition particle consists of a conserved 54-kDa GTPase and a novel 43-kDa chromodomain protein (cpSRP43) that together bind light-harvesting chlorophyll a/b-binding protein (LHCP) to form a soluble targeting complex that is subsequently directed to the thylakoid membrane. Homology-based modeling of cpSRP43 indicates the presence of two previously identified chromodomains along with a third N-terminal chromodomain. Chromodomain deletion constructs were used to examine the role of each chromodomain in mediating distinct steps in the LHCP localization mechanism. The C-terminal chromodomain is completely dispensable for LHCP targeting/integration in vitro. The central chromodomain is essential for both targeting complex formation and integration because of its role in binding the M domain of cpSRP54. The N-terminal chromodomain (CD1) is unnecessary for targeting complex formation but is required for integration. This correlates with the ability of CD1 along with the ankyrin repeat region of cpSRP43 to regulate the GTPase cycle of the cpSRP-receptor complex.}, added-at = {2010-12-14T18:12:02.000+0100}, author = {Goforth, R. L. and Peterson, E. C. and Yuan, J. and Moore, M. J. and Kight, A. D. and Lohse, M. B. and Sakon, J. and Henry, R. L.}, biburl = {https://www.bibsonomy.org/bibtex/2eac79992f1fe8b99c323242415723bd5/pharmawuerz}, endnotereftype = {Journal Article}, interhash = {d8fd63f9c1911dfa2bc701fafd3ed340}, intrahash = {eac79992f1fe8b99c323242415723bd5}, issn = {0021-9258 (Print) 0021-9258 (Linking)}, journal = {J Biol Chem}, keywords = {Acid Amino Ankyrins/chemistry Apoproteins/chemistry Arabidopsis Biological Biosynthesis Chloroplasts/chemistry/metabolism Cloning, Complex/chemistry Data Deletion Electrophoresis, Endoplasmic Fusion GTP Gel Gene Glutathione Hydrolysis II Models, Molecular Particle/chemistry/*physiology Peptides/chemistry Phosphohydrolases/*chemistry Photosystem Plant Polyacrylamide Post-Translational Processing, Protein Proteins/chemistry Recognition Recombinant Reticulum/metabolism Ribosomes/chemistry Sequence Signal Structure, System Techniques Tertiary Thylakoids/metabolism Transduction Transferase/metabolism Transport Two-Hybrid}, month = {Oct 8}, note = {Goforth, Robyn L Peterson, Eric C Yuan, Jianguo Moore, Misty J Kight, Alicia D Lohse, Matthew B Sakon, Joshua Henry, Ralph L P20 RR15569/RR/NCRR NIH HHS/United States Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. United States The Journal of biological chemistry J Biol Chem. 2004 Oct 8;279(41):43077-84. Epub 2004 Aug 2.}, number = 41, pages = {43077-84}, shorttitle = {Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43}, timestamp = {2010-12-14T18:12:11.000+0100}, title = {Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15292240}, volume = 279, year = 2004 }