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PubMed1983

The primary structure of initiation factor IF3 from Bacillus stearothermophilus.

The complete amino acid sequence of the initiation factor IF3 from Bacillus stearothermophilus has been elucidated. This was achieved by splitting the protein with trypsin, Staphylococcus protease or cyanogen bromide. The amino acid sequence was determined by manual Edman degradation, using the DABITC/PITC double-coupling method. The IF3 molecule contains 171 amino acids and has an Mr of 19 677. The sequence was compared to the homologous molecule from Escherichia coli; about 50% of the amino acid residues were found to be identical.

Amino Acid Sequence↗
PubMed1983

A compact three-dimensional crystal form of the large ribosomal subunit from Bacillus stearothermophilus.

A new form of well-ordered three-dimensional crystals of intact 50 S ribosomal subunits from Bacillus stearothermophilus have been obtained. Electron micrographs of positively stained sections of these crystals revealed that the ribosomal particles are packed closely. The cell parameters have been determined. Representative electron micrographs and their computed contoured filtered images are shown.

Crystallization↗
PubMed1984

The amino acid sequence of two small ribosomal proteins from Bacillus stearothermophilus.

The low-Mr proteins (tentatively called protein I and II) were purified from 2 M NaCl extracts of the Bacillus stearothermophilus ribosome. Their amino acid sequences have been determined from the peptides obtained by digestion with trypsin, chymotrypsin, and pepsin, and by cleavage with CNBr, using the micro-DABITC/PITC double-coupling method [FEBS Lett. (1978) 93, 205-214]. Protein I contains 56 residues and has an Mr of 6514. Protein II had 37 residues with an Mr of 4361. The amino acid sequence of protein I shows significant similarity to L32 from E. coli, whereas that of protein II is slightly, if at all, related to ribosomal protein L34 from E. coli.

Amino Acid Sequence↗
PubMed1984

Reconstitution of 50 S ribosomal subunits from Bacillus stearothermophilus with 5 S RNA from spinach chloroplasts and low-Mr RNA from mitochondria of Locusta migratoria and bovine liver.

Reconstitution experiments with 50 S ribosomal subunits from Bacillus stearothermophilus demonstrate that spinach chloroplast 5 S rRNA can be incorporated into the bacterial ribosome and yield biologically active particles, thereby establishing the eubacterial nature of chloroplast 5 S rRNA. In contrast, mitochondria from Locusta migratoria or bovine liver do not appear to contain discrete, low-Mr RNAs, which can replace 5 S rRNA in the functional reconstitution of B. stearothermophilus ribosomes.

Animals↗
PubMed1985

Identity of the metal ligands in the manganese- and iron-containing superoxide dismutases.

Alignment of the amino acid sequence of peptides obtained following digestion of Photobacterium leiognathi iron superoxide dismutase with the known sequence of Bacillus stearothermophilus manganese superoxide dismutase shows that the residues found to form ligands to the manganese are conserved in the iron enzyme. This indicates that the metal ligands in both proteins are identical.

Amino Acid Sequence↗
PubMed1985

Replacement of Mn(III) with Cu(II) in Bacillus stearothermophilus superoxide dismutase. Similarity of the active site to the zinc site of copper/zinc superoxide dismutase.

Copper(II) was substituted for manganese(III) in Bacillus stearothermophilus Mn-superoxide dismutase. The (EPR) spectrum of the Cu(II) is distinctly rhombic, overlapping that of Cu(II) replacing zinc in copper/zinc superoxide dismutase. The copper-cyanide complex of the bacterial enzyme gives an EPR spectrum nearly identical to the cyanide-copper complex of the Cu/Zn enzyme, indicating three nitrogens as metal ligands. These results support the suggestion that metal coordination in B. stearothermophilus Mn-dismutase is a tetrahedral arrangement of three imidazoles and a carboxylate group and indicate copper as a good spectroscopic probe for studying the active site of Mn- and Fe-superoxide dismutases.

Binding Sites↗
PubMed1986

The growth of ordered two-dimensional sheets of 70 S ribosomes from Bacillus stearothermophilus.

Well ordered two-dimensional sheets of intact 70 S ribosomes from Bacillus stearothermophilus have been obtained in vitro using salt-alcohol mixtures. These sheets consist of relatively small unit cells with dimensions of 200 +/- 20 A and 400 +/- 30 A. Diffraction patterns of electron micrographs of these sheets stained with uranyl acetate contain features to 42 A resolution.

Geobacillus stearothermophilus↗
PubMed1986

Mechanism of translational initiation in prokaryotes. Evidence for a direct effect of IF2 on the activity of the 30 S ribosomal subunit.

Initiation factor IF2 from either Escherichia coli or Bacillus stearothermophilus was found to possess the previously undetected property of stimulating the template-dependent ribosomal binding of aminoacyl-tRNAs with free alpha-NH2 groups. IF1, which had no detectable activity alone, was found to stimulate the activity of E. coli IF2 and, to a lesser extent, that of B. stearothermophilus IF2. Since in the absence of ribosomes not even a weak interaction between the two IF2 molecules and the aminoacyl-tRNAs was detected, the present findings indicate that IF2 can act at the ribosomal level stimulating aminoacyl-tRNA binding without prior formation of a binary complex with the aminoacyl-tRNA. IF2 does not appear to open or strengthen a weak A-site binding, but rather to enhance aminoacyl-tRNA binding to a 30 S site equivalent to the P-site by slowing down the rate of aminoacyl-tRNA dissociation from ribosomes.

Escherichia coli↗
PubMed1987

The complete amino acid sequences of the 5 S rRNA binding proteins L5 and L18 from the moderate thermophile Bacillus stearothermophilus ribosome.

The complete amino acid sequences of the 5 S rRNA binding proteins L5 and L18 isolated from ribosomes of the moderate thermophile Bacillus stearothermophilus are presented. This has been achieved by the sequence analysis of peptides derived by enzymatic digestions with trypsin, chymotrypsin, pepsin, and Staphylococcus aureus protease, as well as by chemical cleavage with cyanogen bromide. The proteins L5 and L18 consist of 179 and 120 amino acid residues, and have Mr values of 20,163 and 13,473, respectively. A comparison of the sequences with their counterparts from the Escherichia coli ribosome reveals 59% identical residues for L5, and 53% for L18. For both proteins, the distribution of conserved regions is not random along the protein chains: some regions are highly conserved while others are not. The regions which are conserved during evolution may be important for the interaction with the 5 S rRNA molecule.

Amino Acid Sequence↗
PubMed1987

The complete amino acid sequence of ribosomal protein S12 from Bacillus stearothermophilus.

The amino acid sequence of ribosomal protein S12 from Bacillus stearothermophilus has been completely determined. The sequence data were mainly obtained by manual sequencing of peptides derived from digestion with trypsin, Staphylococcus aureas protease and pepsin. A few overlaps of tryptic peptides were established by DNA sequence analysis of a chromosomal fragment containing the rpsL gene coding for ribosomal protein S12. The protein contains 138 amino acid residues and has an Mr of 15,208. Comparison of this sequence with the sequences of the ribosomal S12 proteins from E. coli as well as from Euglena, tobacco and liverwort chloroplasts shows that 75% of the amino acid residues are identical within the S12 proteins of all four species. Therefore, S12 is the most strongly conserved ribosomal protein known so far.

Amino Acid Sequence↗