PMID:9630516: Difference between revisions

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<span style = 'font-size: large'> '''Farmery, M, Macao, B, Larsson, T and Samuelsson, T'''  (1998) Binding of GTP and GDP induces a significant conformational change in the GTPase domain of Ffh, a bacterial homologue of the SRP 54 kDa subunit.''Biochim. Biophys. Acta'' '''1385''':61-8</span>
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'''Farmery, M, Macao, B, Larsson, T and Samuelsson, T'''  (1998) Binding of GTP and GDP induces a significant conformational change in the GTPase domain of Ffh, a bacterial homologue of the SRP 54 kDa subunit. ''Biochim. Biophys. Acta'' '''1385''':61-8
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!align=left  |Abstract
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The bacterial Ffh protein is homologous to the SRP54 subunit of the signal recognition particle. Ffh plays a key role in the targeting of proteins to the membrane and it is composed of a N-terminal domain (N), a middle GTPase (G) domain and a C-terminal M domain which has binding sites for SRP RNA and signal peptide. The GTP binding and hydrolysis of Ffh is critical to its function. We have used protease digestion to probe the conformation of the Mycoplasma mycoides Ffh N+G domain. In the absence of nucleotide the protein was comparatively sensitive to protease cleavage and we identified sites particularly prone to cleavage in a region near the C-terminus of the GTPase domain. However, in the presence of GTPgammaS or GDP this region is stabilized and the protein adopts a more ordered structure. The pattern of cleavage with GTPgammaS was indistinguishable from that when GDP was bound, indicating that the conformation of the nucleotide-free form is distinct from that when either GTPgammaS or GDP is bound to the protein. The possible functional role of this significant conformational change is discussed.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9630516 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || The bacterial Ffh protein is homologous to the SRP54 subunit of the signal recognition particle. Ffh plays a key role in the targeting of proteins to the membrane and it is composed of a N-terminal domain (N), a middle GTPase (G) domain and a C-terminal M domain which has binding sites for SRP RNA and signal peptide. The GTP binding and hydrolysis of Ffh is critical to its function. We have used protease digestion to probe the conformation of the Mycoplasma mycoides Ffh N+G domain. In the absence of nucleotide the protein was comparatively sensitive to protease cleavage and we identified sites particularly prone to cleavage in a region near the C-terminus of the GTPase domain. However, in the presence of GTPgammaS or GDP this region is stabilized and the protein adopts a more ordered structure. The pattern of cleavage with GTPgammaS was indistinguishable from that when GDP was bound, indicating that the conformation of the nucleotide-free form is distinct from that when either GTPgammaS or GDP is bound to the protein. The possible functional role of this significant conformational change is discussed.
!align=left  |Keywords
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Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Escherichia coli Proteins; GTP Phosphohydrolases/chemistry; GTP Phosphohydrolases/metabolism; Guanosine Diphosphate/metabolism; Guanosine Triphosphate/metabolism; Molecular Sequence Data; Mycoplasma mycoides/enzymology; Protein Structure, Secondary; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Signal Recognition Particle/chemistry; Signal Recognition Particle/metabolism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9630516 PubMed]
 
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Latest revision as of 04:59, 15 September 2013

Citation

Farmery, M, Macao, B, Larsson, T and Samuelsson, T (1998) Binding of GTP and GDP induces a significant conformational change in the GTPase domain of Ffh, a bacterial homologue of the SRP 54 kDa subunit. Biochim. Biophys. Acta 1385:61-8

Abstract

The bacterial Ffh protein is homologous to the SRP54 subunit of the signal recognition particle. Ffh plays a key role in the targeting of proteins to the membrane and it is composed of a N-terminal domain (N), a middle GTPase (G) domain and a C-terminal M domain which has binding sites for SRP RNA and signal peptide. The GTP binding and hydrolysis of Ffh is critical to its function. We have used protease digestion to probe the conformation of the Mycoplasma mycoides Ffh N+G domain. In the absence of nucleotide the protein was comparatively sensitive to protease cleavage and we identified sites particularly prone to cleavage in a region near the C-terminus of the GTPase domain. However, in the presence of GTPgammaS or GDP this region is stabilized and the protein adopts a more ordered structure. The pattern of cleavage with GTPgammaS was indistinguishable from that when GDP was bound, indicating that the conformation of the nucleotide-free form is distinct from that when either GTPgammaS or GDP is bound to the protein. The possible functional role of this significant conformational change is discussed.

Links

PubMed

Keywords

Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Escherichia coli Proteins; GTP Phosphohydrolases/chemistry; GTP Phosphohydrolases/metabolism; Guanosine Diphosphate/metabolism; Guanosine Triphosphate/metabolism; Molecular Sequence Data; Mycoplasma mycoides/enzymology; Protein Structure, Secondary; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Signal Recognition Particle/chemistry; Signal Recognition Particle/metabolism; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin/metabolism

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