Regulation of the GTPase cycle in post-translational signal recognition
particle-based protein targeting involves cpSRP43
R. Goforth, E. Peterson, J. Yuan, M. Moore, A. Kight, M. Lohse, J. Sakon, and R. Henry. J Biol Chem, 279 (41):
43077-84(October 2004)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..
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.
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.
%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
}