Structure, Organization and Evolution of the L1 Equivalent Ribosomal Protein Gene of the Archaebacterium Methanococcus Vannielii

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1990 Feb 25

PMID 2107529

Citations 9

Authors

G Baier

W Piendl

B Redl

G Stoffler

Affiliations

Soon will be listed here.

Abstract

The gene for ribosomal protein MvaL1 from the arachaebacterium Methanococcus vannielii was cloned and characterized. It is clustered together with the genes for MvaL10 and MvaL12, thus is organized in the same order as in E.coli and other archaebacteria. Unexpectedly, analysis of the sequence in front of the MvaL1 gene revealed an ORF of unknown identity, whereas in E.coli, Halobacterium and Sulfolobus solfataricus the gene for the L11 equivalent protein is located in this position. Northern blot analysis revealed a single tricistronic transcript encoding proteins MvaL1, MvaL10 and MvaL12. The 5'-end of the MvaL1-L10-L12 transcript contains a region that has a sequence and structure almost identical to a region on the 23S rRNA which is the putative binding domain for MvaL1, and is highly similar to the E.coli L11-L1 mRNA leader sequence that has been implicated in autogenous translational regulation. Amino acid sequence comparison revealed that MvaL1 shares 30.5% identity with ribosomal protein L1 from E.coli and 41.5% and 33.3% identity with the L1-equivalent proteins from the archaebacteria H.cutirubrum and S.solfataricus respectively.

Citing Articles

RNA chaperone activity of L1 ribosomal proteins: phylogenetic conservation and splicing inhibition.

Ameres S, Shcherbakov D, Nikonova E, Piendl W, Schroeder R, Semrad K Nucleic Acids Res. 2007; 35(11):3752-63.

PMID: 17517772 PMC: 1920258. DOI: 10.1093/nar/gkm318.

Ribosomal protein L1 recognizes the same specific structural motif in its target sites on the autoregulatory mRNA and 23S rRNA.

Nevskaya N, Tishchenko S, Gabdoulkhakov A, Nikonova E, Nikonov O, Nikulin A Nucleic Acids Res. 2005; 33(2):478-85.

PMID: 15659579 PMC: 548342. DOI: 10.1093/nar/gki194.

Archaea and the prokaryote-to-eukaryote transition.

Brown J, Doolittle W Microbiol Mol Biol Rev. 1997; 61(4):456-502.

PMID: 9409149 PMC: 232621. DOI: 10.1128/mmbr.61.4.456-502.1997.

Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus.

Nikonov S, Nevskaya N, Eliseikina I, Fomenkova N, Nikulin A, Ossina N EMBO J. 1996; 15(6):1350-9.

PMID: 8635468 PMC: 450039.

Autogenous translational regulation of the ribosomal MvaL1 operon in the archaebacterium Methanococcus vannielii.

Hanner M, Mayer C, Kohrer C, Golderer G, Grobner P, Piendl W J Bacteriol. 1994; 176(2):409-18.

PMID: 8288536 PMC: 205064. DOI: 10.1128/jb.176.2.409-418.1994.

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