The first 37 residues are sufficient for dimerization of ribosomal L7/L12 protein

Gudkov, A.T.; Budovskaya, Yelena V.; Sherstobaeva, N.M.

doi:10.1016/0014-5793(95)00564-p

Cited by 15 publications

(23 citation statements)

References 20 publications

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“…The L7/L12 dimers are associated with the ribosome by their dNTDs via protein L10 (6,19,61). Although the spatial structure of the protein L10 is not know at present, it is established that hydrophobic interactions are responsible for binding the L7/L12 dNTD to the protein L10 (62) and that the dNTD is mobile in the complex with L10 (19).…”

Section: Unique Flexible Structure Of L7/l12 Dimer Is a Key Feature Fmentioning

confidence: 99%

From Structure and Dynamics of Protein L7/L12 to Molecular Switching in Ribosome

Bocharov

Sobol

Павлов

et al. 2004

Journal of Biological Chemistry

106

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Based on the 1 H-15 N NMR spectroscopy data, the three-dimensional structure and internal dynamic properties of ribosomal protein L7 from Escherichia coli were derived. The structure of L7 dimer in solution can be described as a set of three distinct domains, tumbling rather independently and linked via flexible hinge regions. The dimeric N-terminal domain (residues 1-32) consists of two antiparallel ␣-␣-hairpins forming a symmetrical four-helical bundle, whereas the two identical C-terminal domains (residues 52-120) adopt a compact ␣/␤-fold. There is an indirect evidence of the existence of transitory helical structures at least in the first part (residues 33-43) of the hinge region. Combining structural data for the ribosomal protein L7/L12 from NMR spectroscopy and x-ray crystallography, it was suggested that its hinge region acts as a molecular switch, initiating "ratchet-like" motions of the L7/L12 stalk with respect to the ribosomal surface in response to elongation factor binding and GTP hydrolysis. This hypothesis allows an explanation of events observed during the translation cycle and provides useful insights into the role of protein L7/L12 in the functioning of the ribosome.

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Section: Unique Flexible Structure Of L7/l12 Dimer Is a Key Feature Fmentioning

confidence: 99%

From Structure and Dynamics of Protein L7/L12 to Molecular Switching in Ribosome

Bocharov

Sobol

Павлов

et al. 2004

Journal of Biological Chemistry

106

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“…Recently the head-to-head orientation of the subunits in the dimer has been suggested in studies of functional activity of the L7/L12 Cys38 mutant dimer [7]. Oxidation of all the three (14, 17 and 26) methionine residues of L7/L 12 disrupts its dimer structure [8,9].…”

Section: Introductionmentioning

confidence: 99%

Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution

1996

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Topology of the secondary structure elements of ribosomal protein L7/L12 has been studied. The sequential assignment was obtained for main and side chain resonances. This allows the overall secondary structure to be described. The results of high resolution NMR studies show that dimer of the ribosomal protein L7/L12 from Escheriehia coli has a parallel (head-tohead) orientation of subunits, and N-terminal domain (NTD, residues Serl--Ser33) has no contacts with the C-terminal domain (CTD, residues Lys51-Lysl20). The NMR data for CTD are in line with crystallographic structure. The flexible interdomain (hinge) region (residues Ala34-Glu50) has an unordered structure, the Pro44 forming both cis and trans peptide bonds. Due to the conformational exchange the intensities of the peaks from the NTD are low. The conformation of the NTD, which is responsible for the formation of the L7/L12 dimer, is a-helical hairpin. The NTD dimer forms an antiparallel four-t~-helix bundle.

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“…The protein consists of three domains. The N-terminal domain is required for dimer formation and for anchoring the protein to the ribosome by binding to ribosomal protein L10, whereas the C-terminal domain is involved in factor binding (28,29). The hinge region enables independent movement of the C-terminal domains relative to each other and to the N-terminal domains (30,31).…”

mentioning

confidence: 99%

Stimulation of the GTPase Activity of Translation Elongation Factor G by Ribosomal Protein L7/12

Savelsbergh

Mohr

Wilden

et al. 2000

Journal of Biological Chemistry

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Elongation factors (EFs) Tu and G are GTPases that have important functions in protein synthesis. The low intrinsic GTPase activity of both factors is strongly stimulated on the ribosome by unknown mechanisms. Here we report that isolated ribosomal protein L7/12 strongly stimulates GTP hydrolysis by EF-G, but not by EF-Tu, indicating a major contribution of L7/12 to GTPase activation of EF-G on the ribosome. The effect is due to the acceleration of the catalytic step because the rate of GDP-GTP exchange on EF-G, as measured by rapid kinetics, is much faster than the steady-state GTPase rate. The unique, highly conserved arginine residue in the C-terminal domain of L7/12 is not essential for the activation, excluding an "arginine finger"-type mechanism. L7/12 appears to function by stabilizing the GTPase transition state of EF-G.

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The first 37 residues are sufficient for dimerization of ribosomal L7/L12 protein

Cited by 15 publications

References 20 publications

From Structure and Dynamics of Protein L7/L12 to Molecular Switching in Ribosome

From Structure and Dynamics of Protein L7/L12 to Molecular Switching in Ribosome

Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution

Stimulation of the GTPase Activity of Translation Elongation Factor G by Ribosomal Protein L7/12

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