The complete amino acid sequence of ribosomal protein H‐S11 from the archaebacterium <i>Halobacterium marismortui</i>

Arndt, Evelyn; Breithaupt, Gabriele; Kimura, Makoto

doi:10.1016/0014-5793(86)80090-4

Cited by 28 publications

(9 citation statements)

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“…Hm-S12 He-S.13 Fl Hm-S17 E&9 Gl H&20 EC-S21 a Described in this paper b Arndt et al (211 ' Yaguchi et al [20] cutirubrum [ 181 and H. marismortui [21]. A spot corresponding to protein C is absent in the H. cutirubrum pattern and is labeled S2 in the N, mari~mortui proteins.…”

Section: Identification and Amino-terminal Sequences Of The Isolated mentioning

confidence: 96%

“…A spot corresponding to protein C is absent in the H. cutirubrum pattern and is labeled S2 in the N, mari~mortui proteins. The nomenclature used by Matheson and co-workers [20] and Kimura [21], although both based on 2D gels, are different from each other. For comparison, we list the names of the isolated proteins in both systems of nomenclature (table 1).…”

Section: Identification and Amino-terminal Sequences Of The Isolated mentioning

confidence: 99%

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Purification and characterization of ribosomal proteins from the 30 S subunit of the extreme halophile Halobacterium marismortui

Shoham¹,

Dijk²,

Reinhardt³

et al. 1986

FEBS Letters

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Ribosomal proteins were extracted from 30 S subunits of Halobacterium marismortui under native conditions. Their separation was based on gel filtration and hydrophobic chromatography, performed at a concentration of 3.2 M KC1 to avoid denaturation. A total of nine proteins were isolated, purified and identified by partial amino-terminal sequences and two-dimensiona gel electrophoresis. There is a high degree of sequence homology with 30 S proteins from H. cutirubrum, and also some with 30 S proteins of eubacteria. Proton NMR data indicate unfolding of the proteins in low salt. One of the proteins, however, retains its secondary structure at a salt concentration as low as 0.1 M NaCl, and even in 8 M urea. One reason for this outstanding stability could be the high proportion (50%) of /?-structure in this protein as determined from circular dichroism measurements. In general, there is a higher B-sheet content than for 30 S proteins from Escherichia eoii. Measurements of Stokes radii indicate several of the proteins to have a rather elongated shape. One of these is a complex consisting of L3/L4 and L20, similar to the LI-complex from E. co&. The presence of this 50 S compiex in the preparation of the small subunit suggests a location on the interface between the subunits.(Halobacterium) Ribosomai protein 30 S subunit

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Section: Identification and Amino-terminal Sequences Of The Isolated mentioning

confidence: 96%

Section: Identification and Amino-terminal Sequences Of The Isolated mentioning

confidence: 99%

Purification and characterization of ribosomal proteins from the 30 S subunit of the extreme halophile Halobacterium marismortui

Shoham¹,

Dijk²,

Reinhardt³

et al. 1986

FEBS Letters

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“…For instance, a halobacterial ribosomal small subunit protein from H . murismortui, Sl 1, consists of 155 amino acid residues, whereas its equivalents in eubacterial ribosomes, E. coli S15 and B. stearothermophilus S15, contain only 87 and 88 amino acid residues, respectively [3]. H .…”

Section: Comparison Of' [He Amino Acid Sequencesmentioning

confidence: 99%

Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins

Hatakeyama

Kaufmann

Schroeter

et al. 1989

European Journal of Biochemistry

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The complete amino acid sequences of ribosomal proteins L9, L20, L21/22, L24 and L32 from the archaebacterium Halobacterium marismorlui were determined. The comparison of the sequences of these proteins with those from other organisms revealed that proteins L21/22 and L24 are homologous to ribosomal protein Yrp29 from yeast and L19 from rat, respectively, and that H . marismortui L20 is homologous to L30 from eubacteria. H. marismortui ribosomal protein L9 showed sequence homology to both L29 from yeast and L15 from eubacteria. No homologous protein was found for H. marismortui L32. These results are discussed with respect to the phylogenetic relationship between eubacteria, archaebacteria and eukaryotes.Archaebacteria were postulated as a third kingdom besides eubacteria and eukaryotes [l]. Since ribosomes occur in all organisms and consist of many components they are ideal objects for studies on phylogenetic relationships between these kingdoms. We have determined the amino acid sequences of a number of ribosomal proteins isolated from the archaebacterium Halobacterium marismortui [2 -91. Comparison of these amino acid sequcnces with those from other organisms has revealed that halobacterial proteins are heterogeneous with respect to the primary structures. Some of the halobacterial ribosomal proteins are homologous only to eubacterial or to eukaryotic proteins, some are homologous to both eubacterial and eukaryotic proteins, whereas others show no homology to any ribosomal proteins so far scquenced.The determination of the amino acid sequences of ribosomal proteins from halobacteria is not only valuable with respect to phylogenetic relationships among organisms but is also important for crystallographic investigations on these ribosomes. Large and well-ordered three-dimensional crystals of intact 50s ribosomal subunits which diffracted to 0.6 nm resolution in a synchrotron beam were obtained from H . marismortui [lo]. Knowledge of the primary structures of the ribosomal components is helpful for the current studies on heavy-atom derivatives and for the crystallographic data evaluation.In this paper, we describe the primary structures of the five ribosomal proteins L9, L20, L21/22, L24 and L32 of H . marismortui, which have recently been isolated in sufficient amounts for sequence determination, and their structural relationships to the counterparts in cubacterial and eukaryotic ribosomes. MATERIALS AND METHODS Purvkation of'rihosomnl proteinsThe ribosomes and their subunits from H . marismortui were prepared as reported previously [l 11. The ribosomal proteins were extracted from 50s ribosomal subunits according to [I 21 and separated by ion-exchange chromatography using DEAE-cellulose in 75 mM Tris/citrate buffer, pH 7.9, containing 30% dimethylformamide 161. Elution was performed by a linear gradient of 0-0.3 M KCI, followed by elution with 0.5 M KC1 in the same buffer. The fractions were pooled after detection of proteins by SDSjPAGE [I31 and dialyzed against water. Proteins were separated either on a TSK ...

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“…The ribosomal proteins were purified using a method similar to that described for the purification of the H. marismortui 30s ribosomal proteins [2]. Extracted proteins (fractions S-1 and S-2) were dialyzed against 75 mM Tris/citrate buffer (pH 7.9) containing 30% dimethylformamide and applied to a DEAE-cellulose column (2.5 x 25 cm) previously equilibrated with the same buffer.…”

Section: Purification Of Proteinsmentioning

confidence: 99%

Complete amino acid sequences of the ribosomal proteins L25, L29 and L31 from the archaebacterium Halobacterium marismortui

Hatakeyama

Kimura

1988

European Journal of Biochemistry

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Ribosomal proteins were extracted from 50s ribosomal subunits of the archaebacterium Halobacterium marismortui by decreasing the concentration of Mg2+ and K', and the proteins were separated and purified by ion-exchange column chromatography on DEAE-cellulose. Ten proteins were purified to homogeneity and three of these proteins were subjected to sequence analysis. The complete amino acid sequences of the ribosomal proteins L25, L29 and L31 were established by analyses of the peptides obtained by enzymatic digestion with trypsin, Staphylococcus aureus protease, chymotrypsin and lysylendopeptidase. Proteins L25, L29 and L31 consist of 84, 115 and 95 amino acid residues with the molecular masses of 9472 Da, 12293 Da and 10418 Da respectively. A comparison of their sequences with those of other large-ribosomal-subunit proteins from other organisms revealed that protein L25 from H. marismortui is homologous to protein L23 from Escherichia coli (34.6%), Bacillus stearothermophilus (41 .So/,), and tobacco chloroplasts (16.3%) as well as to protein L25 from yeast (38.0%). Proteins L29 and L31 do not appear to be homologous to any other ribosomal proteins whose structures are so far known.In previous papers [l -41 we have reported the complete amino acid sequences of a number of proteins from 30s ribosomal subunits from the archaebacterium Halobacterium marismortui. The rationale of this ongoing investigation is not only to examine the evolutionary origin of the halobacterial ribosomal proteins, but also to evaluate the amino acid changes which have allowed the adaptation into a high-salt environment. A comparison of homologous proteins from distantly related organisms also provides useful information about functionally and/or structurally important sites, since important regions are expected to be conserved through evolution.In addition to our primary structural analyses, studies on the spatial structure of H. marismortui ribosomal proteins [ S ] and intact ribosomal subunits [6] are now in progress at our institute. In particular, Makowski et al.[7] have performed X-ray diffraction studies on crystals of the large ribosomal subunits from H. marismortui which diffract to 0.6-nm resolution.As a part of this investigation on the structure of the halobacterial ribosomal proteins and also to facilitate the structural analysis on crystals of the intact large ribosomal subunits from H. marisrplortui, we are now extending the sequence analyses to the proteins of the 50s ribosomal subunit from this halophilic bacterium. At present, a number of 50s-ribosomal-subunit proteins have been purified by ion-exchange chromatography for sequence analysis (unpublished results). In this paper we describe the isolation and complete amino acid sequences of ribosomal proteins L25, L29 and L31 from H. marismortui and present their relationship with other ribosomal proteins whose primary structures have been determined.

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The complete amino acid sequence of ribosomal protein H‐S11 from the archaebacterium Halobacterium marismortui

Cited by 28 publications

References 30 publications

Purification and characterization of ribosomal proteins from the 30 S subunit of the extreme halophile Halobacterium marismortui

Purification and characterization of ribosomal proteins from the 30 S subunit of the extreme halophile Halobacterium marismortui

Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins

Complete amino acid sequences of the ribosomal proteins L25, L29 and L31 from the archaebacterium Halobacterium marismortui

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