Nucleotide sequence of a gene cluster encoding NusG and the L11-L1-L10-L12 ribosomal proteins from the thermophilic archaeon Sulfolobus solfataricus

Geiger, Markus; Gröbner, Peter; Piendl, Wolfgang

doi:10.1016/s0167-4838(97)00073-3

Cited by 4 publications

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“…1) resulting in complete failure to interact with MvaL1 [9]. A comparison of the DNA-deduced amino acid sequences of the L1 proteins from M. vannielii (MvaL1) [29], M. jannaschii (MjaL1) [10], M. thermolithotrophicus (MthL1; Linhart and Piendl, unpublished results; GenBank accession number AF044919), S. solfataricus (SsoL1) [11], E. coli (EcoL1) [30] and T. thermophilus (TthL1) [31] reveals a sequence identity of 23.5Ϫ79.8 % ( Table 2). L1 from the mesophilic Archaeon M. vannielii shares 64.8 % and 79.8 % sequence identity with its equivalents from the hyperthermophilic M. jannaschii and the thermophilic M. thermolithotrophicus, respectively, and only 37.1 % identity with L1 from the hyperthermophilic Archaeon S. solfataricus.…”

Section: Resultsmentioning

confidence: 99%

“…MvaL1 exhibits a sequence identity of about 24% with its bacterial counterparts. When compared to the bacterial L1 proteins, the archaeal sequences are mainly characterized by an N-terminus which is 14Ϫ18 amino acids shorter and by an insertion of seven amino acids at positions 112Ϫ118 [11,33].…”

Section: Resultsmentioning

confidence: 99%

“…The nucleotide sequence of the L1-L10-L12 gene cluster is available from the hyperthermophilic M. jannaschii (optimal growth temperature 85°C; the complete genome sequence has been published recently [10]) and from M. thermolithotrophicus (Linhart and Piendl, unpublished results; the nucleotide sequence is available in the GenBank DNA sequence data base under accession number AF044919), which grows optimally at 65°C. Furthermore, we have included in our pFDX500 derivative containing the gene for the rare tRNA Arg AGA/AGG of E. coli [19] studies protein L1 from the Crenarchaeon Sulfolobus solfataricus (optimal growth temperature 85°C) [11] and from two Bacteria, the mesophilic E. coli and the thermophilic Thermus thermophilus (optimal growth temperature 75°C). We have used filter-binding assays to examine the interactions between ribosomal L1 proteins from the organisms mentioned above with specific L1-binding sites on 23S rRNA and mRNA.…”

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Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1‐binding sites on 23S rRNA and mRNA

Köhrer

Mayer

Neumair

et al. 1998

European Journal of Biochemistry

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In Bacteria and Archaea (formerly Archaebacteria) ribosomal protein L1 has a dual function, as a primary rRNA-binding protein and as a translational repressor which binds to its own mRNA. The L1-binding site on the mRNA exhibits high similarity in both sequence and secondary structure to the binding site for L1 on the 23 S rRNA. A sensitive membrane-filter-binding assay has been used to examine the interactions between ribosomal L1 proteins from different archaeal and bacterial species, and 23S rRNA and mRNA fragments from Methanococcus vannielii containing the MvaL1-binding site. Under standard conditions (0°C, pH 7.5, 20 mM Mg 2ϩ , 500 mM KCl), the apparent dissociation constant Kd of the homologous MvaL1-23S rRNA complex is 5 nM, the apparent dissociation constant K d of the MvaL1-mRNA complex is 0.15 µM. L1 proteins from Escherichia coli (EcoL1) and from the thermophilic Bacterium Thermus thermophilus (TthL1), and from the thermophilic Archaea Methanococcus thermolithotrophicus (MthL1), Methanococcus jannaschii (MjaL1), and Sulfolobus solfataricus (SsoL1) were tested for their affinity to the specific L1-binding sites on the 23 S rRNA and mRNA. In general, the affinity of L1 proteins from thermophilic species to the binding sites on both 23 S rRNA and mRNA is about one order of magnitude higher than that of their mesophilic counterparts. This stronger protein-RNA interaction might make a substantial contribution to the thermal tolerance of ribosomes in thermophilic organisms.Keywords : RNA-ribosomal protein L1 interaction ; filter-binding assay; Archaea ; mesophilic and thermophilic Methanococcus.Over the last two decades, a growing number of organisms living at temperatures close to or above the boiling point of water have been discovered. With a few (bacterial) exceptions, they have been classified as Archaea [1]. The adaption of these thermophilic organisms requires, amongst a number of modifications at the molecular level, a structural response of the ribosomes to ensure both high efficiency and high accuracy of the translational machinery at high temperatures. To date, very little is known about the molecular mechanisms regulating the thermal stabilization of ribosomes. Only for the hyperthermophilic Crenarchaeon, Sulfolobus solfataricus, have the mechanisms involved in the thermal stabilization of ribosomes been investigated in some detail. The heat stability of both 50S and 30S ribosomal subunits appears to be accounted for by the intrinsic stabilization of the helical rRNA domains (by a higher number of GϩC base pairs) and by a more extensive interaction between ribosomal proteins and rRNA [2Ϫ4].Ribosomal protein L1 from mesophilic and (hyper)thermophilic organisms is particularly suitable to study the specific interaction with RNA. In Bacteria and Archaea, ribosomal protein L1 has a dual function as a primary rRNA-binding protein and as a translational repressor. The primary and secondary structure of the L1-binding region on the 23S and 28S rRNA is highly conserved in Bacteria, Archaea and Eukarya ...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1‐binding sites on 23S rRNA and mRNA

Köhrer

Mayer

Neumair

et al. 1998

European Journal of Biochemistry

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“…coli (Egebjerg et al ., 1991). When compared with bacterial L1 proteins, the archaeal sequences are mainly characterized by an N‐terminus, which is 14–18 amino acids shorter (Geiger et al ., 1997). Interestingly, the extended bacterial L1 N‐terminus is involved in RNA binding (Eliseikina et al ., 1996).…”

Section: Discussionmentioning

confidence: 99%

MvaL1 autoregulates the synthesis of the three ribosomal proteins encoded on the MvaL1 operon of the archaeon Methanococcus vannielii by inhibiting its own translation before or at the formation of the first peptide bond

Mayer

Köhrer

Gröbner

et al. 1998

Molecular Microbiology

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SummaryThe control of ribosomal protein synthesis has been investigated extensively in Eukarya and Bacteria. In Archaea, only the regulation of the MvaL1 operon (encoding ribosomal proteins MvaL1, MvaL10 and MvaL12) of Methanococcus vannielii has been studied in some detail. As in Escherichia coli, regulation takes place at the level of translation. MvaL1, the homologue of the regulatory protein L1 encoded by the L11 operon of E. coli, was shown to be an autoregulator of the MvaL1 operon. The regulatory MvaL1 binding site on the mRNA is located about 30 nucleotides downstream of the ATG start codon, a sequence that is not in direct contact with the initiating ribosome. Here, we demonstrate that autoregulation of MvaL1 occurs at or before the formation of the first peptide bond of MvaL1. Specific interaction of purified MvaL1 with both 23S RNA and its own mRNA is confirmed by filter binding studies. In vivo expression experiments reveal that translation of the distal MvaL10 and MvaL12 cistrons is coupled to that of the MvaL1 cistron. A mRNA secondary structure resembling a canonical L10 binding site and preliminary in vitro regulation experiments had suggested a co-regulatory function of MvaL10, the homologue of the regulatory protein L10 of the ␤-operon of E. coli. However, we show that MvaL10 does not have a regulatory function.

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Towards a Reconstruction of Ancestral Genomes by Gene Cluster Alignment

Wächtershäuser¹

1998

Systematic and Applied Microbiology

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Nucleotide sequence of a gene cluster encoding NusG and the L11-L1-L10-L12 ribosomal proteins from the thermophilic archaeon Sulfolobus solfataricus

Cited by 4 publications

References 30 publications

Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1‐binding sites on 23S rRNA and mRNA

Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1‐binding sites on 23S rRNA and mRNA

MvaL1 autoregulates the synthesis of the three ribosomal proteins encoded on the MvaL1 operon of the archaeon Methanococcus vannielii by inhibiting its own translation before or at the formation of the first peptide bond

Towards a Reconstruction of Ancestral Genomes by Gene Cluster Alignment

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