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Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome

Mulder, Frans LU ; Bouakaz, L; Lundell, Anna; Venkataramana, M; Liljas, Anders LU ; Akke, Mikael LU and Sanyal, Suparna LU (2004) In Biochemistry 43(20). p.5930-5936
Abstract
During translation, the ribosome and several of its constituent proteins undergo structural transitions between different functional states. Protein L12, present in four copies in prokaryotic ribosomes, forms a flexible "stalk" with key functions in factor-dependent GTP hydrolysis during translocation. Here we have used heteronuclear NMR spectroscopy to characterize L12 conformation and dynamics in solution and on the ribosome. Isolated L 12 forms a symmetric dimer mediated by the N-terminal domains (NTDs), to which each C-terminal domain (CTD) is connected via an unstructured hinge segment. The overall structure can be described as three ellipsoids joined by flexible linkers. No persistent contacts are seen between the two CTDs, or... (More)
During translation, the ribosome and several of its constituent proteins undergo structural transitions between different functional states. Protein L12, present in four copies in prokaryotic ribosomes, forms a flexible "stalk" with key functions in factor-dependent GTP hydrolysis during translocation. Here we have used heteronuclear NMR spectroscopy to characterize L12 conformation and dynamics in solution and on the ribosome. Isolated L 12 forms a symmetric dimer mediated by the N-terminal domains (NTDs), to which each C-terminal domain (CTD) is connected via an unstructured hinge segment. The overall structure can be described as three ellipsoids joined by flexible linkers. No persistent contacts are seen between the two CTDs, or between the NTD and CTD in the L12 dimer in solution. In the H-1-N-15 HSQC spectrum of the Escherichia coli 70S ribosome, a single set of cross-peaks are observed for residues 40-120 of L12, the intensities of which correspond to only two of four protein copies. The structure of the CTDs observed on the ribosome is indistinguishable from that of isolated L12. These results indicate that two CTDs with identical average structures are mobile and extend away from the ribosome, while the other two copies most likely interact tightly with the ribosome even in the absence of translational factors. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
43
issue
20
pages
5930 - 5936
publisher
The American Chemical Society
external identifiers
  • wos:000221535400002
  • pmid:15147176
  • scopus:2442662936
ISSN
0006-2960
DOI
10.1021/bi0495331
language
English
LU publication?
yes
id
477a860e-a5cc-4d91-b0a4-029a2dc6cc2f (old id 139400)
date added to LUP
2007-06-29 14:05:58
date last changed
2017-10-22 03:56:26
@article{477a860e-a5cc-4d91-b0a4-029a2dc6cc2f,
  abstract     = {During translation, the ribosome and several of its constituent proteins undergo structural transitions between different functional states. Protein L12, present in four copies in prokaryotic ribosomes, forms a flexible "stalk" with key functions in factor-dependent GTP hydrolysis during translocation. Here we have used heteronuclear NMR spectroscopy to characterize L12 conformation and dynamics in solution and on the ribosome. Isolated L 12 forms a symmetric dimer mediated by the N-terminal domains (NTDs), to which each C-terminal domain (CTD) is connected via an unstructured hinge segment. The overall structure can be described as three ellipsoids joined by flexible linkers. No persistent contacts are seen between the two CTDs, or between the NTD and CTD in the L12 dimer in solution. In the H-1-N-15 HSQC spectrum of the Escherichia coli 70S ribosome, a single set of cross-peaks are observed for residues 40-120 of L12, the intensities of which correspond to only two of four protein copies. The structure of the CTDs observed on the ribosome is indistinguishable from that of isolated L12. These results indicate that two CTDs with identical average structures are mobile and extend away from the ribosome, while the other two copies most likely interact tightly with the ribosome even in the absence of translational factors.},
  author       = {Mulder, Frans and Bouakaz, L and Lundell, Anna and Venkataramana, M and Liljas, Anders and Akke, Mikael and Sanyal, Suparna},
  issn         = {0006-2960},
  language     = {eng},
  number       = {20},
  pages        = {5930--5936},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome},
  url          = {http://dx.doi.org/10.1021/bi0495331},
  volume       = {43},
  year         = {2004},
}