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Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family

Nevskaya, Natasha; Tischenko, S; Fedorov, R; Al-Karadaghi, Salam LU ; Liljas, Anders LU ; Kraft, A; Piendl, W; Garber, M and Nikonov, S (2000) In Structure 8(4). p.363-371
Abstract
Background: L1 is an important primary rRNA-binding protein, as well as a translational repressor that binds mRNA. It was shown that L1 proteins from some bacteria and archaea are functionally interchangeable within the ribosome and in the repression of translation. The crystal structure of bacterial L1 from Thermus thermophilus (TthL1) has previously been determined.



Results: We report here the first structure of a ribosomal protein from archaea, L1 from Methanococcus jannaschii (MjaL1). The overall shape of the two-domain molecule differs dramatically from that of its bacterial counterpart (TthL1) because of the different relative orientations of the domains. Two strictly conserved regions of the amino acid sequence,... (More)
Background: L1 is an important primary rRNA-binding protein, as well as a translational repressor that binds mRNA. It was shown that L1 proteins from some bacteria and archaea are functionally interchangeable within the ribosome and in the repression of translation. The crystal structure of bacterial L1 from Thermus thermophilus (TthL1) has previously been determined.



Results: We report here the first structure of a ribosomal protein from archaea, L1 from Methanococcus jannaschii (MjaL1). The overall shape of the two-domain molecule differs dramatically from that of its bacterial counterpart (TthL1) because of the different relative orientations of the domains. Two strictly conserved regions of the amino acid sequence, each belonging to one of the domains and positioned close to each other in the interdomain cavity of TthL1, are separated by about 25 Å in MjaL1 owing to a significant opening of the structure. These regions are structurally highly conserved and are proposed to be the specific RNA-binding sites.



Conclusions: The unusually high RNA-binding affinity of MjaL1 might be explained by the exposure of its highly conserved regions. The open conformation of MjaL1 is strongly stabilized by nonconserved interdomain interactions and suggests that the closed conformations of L1 (as in TthL1) open upon RNA binding. Comparison of the two L1 protein structures reveals a high conformational variability of this ribosomal protein. Determination of the MjaL1 structure offers an additional variant for fitting the L1 protein into electron-density maps of the 50S ribosomal subunit. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Archaeal ribosomal protein L1, Methanococcus jannaschii, Ribosomes, RNA-binding protein, X-ray crystallography
in
Structure
volume
8
issue
4
pages
363 - 371
publisher
Cell Press
external identifiers
  • scopus:0034655657
ISSN
0969-2126
DOI
10.1016/S0969-2126(00)00116-7
language
English
LU publication?
yes
id
efb91d3b-e7f7-47dc-8ead-f7d6267f8966 (old id 948670)
date added to LUP
2008-01-25 12:54:07
date last changed
2017-02-26 03:25:11
@article{efb91d3b-e7f7-47dc-8ead-f7d6267f8966,
  abstract     = {Background: L1 is an important primary rRNA-binding protein, as well as a translational repressor that binds mRNA. It was shown that L1 proteins from some bacteria and archaea are functionally interchangeable within the ribosome and in the repression of translation. The crystal structure of bacterial L1 from Thermus thermophilus (TthL1) has previously been determined.<br/><br>
<br/><br>
Results: We report here the first structure of a ribosomal protein from archaea, L1 from Methanococcus jannaschii (MjaL1). The overall shape of the two-domain molecule differs dramatically from that of its bacterial counterpart (TthL1) because of the different relative orientations of the domains. Two strictly conserved regions of the amino acid sequence, each belonging to one of the domains and positioned close to each other in the interdomain cavity of TthL1, are separated by about 25 Å in MjaL1 owing to a significant opening of the structure. These regions are structurally highly conserved and are proposed to be the specific RNA-binding sites.<br/><br>
<br/><br>
Conclusions: The unusually high RNA-binding affinity of MjaL1 might be explained by the exposure of its highly conserved regions. The open conformation of MjaL1 is strongly stabilized by nonconserved interdomain interactions and suggests that the closed conformations of L1 (as in TthL1) open upon RNA binding. Comparison of the two L1 protein structures reveals a high conformational variability of this ribosomal protein. Determination of the MjaL1 structure offers an additional variant for fitting the L1 protein into electron-density maps of the 50S ribosomal subunit.},
  author       = {Nevskaya, Natasha and Tischenko, S and Fedorov, R and Al-Karadaghi, Salam and Liljas, Anders and Kraft, A and Piendl, W and Garber, M and Nikonov, S},
  issn         = {0969-2126},
  keyword      = {Archaeal ribosomal protein L1,Methanococcus jannaschii,Ribosomes,RNA-binding protein,X-ray crystallography},
  language     = {eng},
  number       = {4},
  pages        = {363--371},
  publisher    = {Cell Press},
  series       = {Structure},
  title        = {Archaeal ribosomal protein L1: the structure provides new insights into RNA binding of the L1 protein family},
  url          = {http://dx.doi.org/10.1016/S0969-2126(00)00116-7},
  volume       = {8},
  year         = {2000},
}