Ribosomal proteins in halobacteria

1989 ◽  
Vol 35 (1) ◽  
pp. 195-199 ◽  
Author(s):  
Makoto Kimura ◽  
Evelyn Arndt ◽  
Tomomitsu Hatakeyama ◽  
Tamiko Hatakeyama ◽  
Junko Kimura
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dna Sequencing ◽  
Glutamic Acid ◽  
Ribosomal Proteins ◽  
Chemical Method ◽  
Amino Acid Sequences ◽  
Protein Sequencing ◽  
Arginine Residues

The amino acid sequences of 16 ribosomal proteins from archaebacterium Halobacterium marismortui have been determined by a direct protein chemical method. In addition, amino acid sequences of three proteins, S11, S18, and L25, have been established by DNA sequencing of their genes as well as by protein sequencing. Comparison of their sequences with those of ribosomal proteins from other organisms revealed that proteins S14, S16, S19, and L25 are related to both eukaryotic and eubacterial ribosomal proteins, being more homologous to eukaryotic than eubacterial counterparts, and proteins S12, S15, and L16 are related to only eukaryotic ribosomal proteins. Furthermore, some proteins are found to be similar to only eubacterial proteins, whereas other proteins show no homology to any other known ribosomal proteins. Comparisons of amino acid compositions between halophilic and nonhalophilic ribosomal proteins revealed that halophilic proteins gain asparatic and glutamic acid residues and significantly lose lysine and arginine residues. In addition, halophilic proteins seem to lose isoleucine as compared with Escherichia coli ribosomal proteins.Key words: halobacteria, ribosomal proteins, amino acid sequence.

scholarly journals Diarrhea-Inducing Activity of Avian Rotavirus NSP4 Glycoproteins, Which Differ Greatly from Mammalian Rotavirus NSP4 Glycoproteins in Deduced Amino Acid Sequence, in Suckling Mice

2002 ◽  
Vol 76 (11) ◽  
pp. 5829-5834 ◽  
Author(s):  
Yoshio Mori ◽  
Mohammed Ali Borgan ◽  
Naoto Ito ◽  
Makoto Sugiyama ◽  
Nobuyuki Minamoto
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Suckling Mice

ABSTRACT Avian rotavirus NSP4 glycoproteins expressed in Escherichia coli acted as enterotoxins in suckling mice, as did mammalian rotavirus NSP4 glycoproteins, despite great differences in the amino acid sequences. The enterotoxin domain of PO-13 NSP4 exists in amino acid residues 109 to 135, a region similar to that reported in SA11 NSP4.

Purification, properties, and N-terminal amino acid sequence of certain 50S ribosomal subunit proteins from the archaebacterium Halobacterium cutirubrum

1984 ◽  
Vol 62 (6) ◽  
pp. 426-433 ◽  
Author(s):  
Alastair T. Matheson ◽  
Makoto Yaguchi ◽  
Patricia Christensen ◽  
C. Fernand Rollin ◽  
Sadiq Hasnain
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Homology ◽  
Ribosomal Proteins ◽  
Large Subunit ◽  
Ribosomal Subunit ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

Sixteen ribosomal proteins (r-proteins) from the 50S ribosomal subunit of the archaebacterium Halobacterium cutirubrum have been purified and their amino acid composition and partial N-terminal amino acid sequence have been determined. These proteins as a group are much more acidic than the large subunit r-proteins from eubacteria or eukaryotes. Little sequence homology is evident between the 50S subunit archaebacterial r-proteins and the equivalent proteins from the eubacterium Escherichia coli.

scholarly journals Amino acid sequence of the Bb fragment from human complement Factor B. Alignment of the cyanogen bromide-cleavage peptides

1983 ◽  
Vol 209 (1) ◽  
pp. 51-60 ◽  
Author(s):  
J Gagnon ◽  
D L Christie
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Factor ◽  
Alternative Pathway ◽  
Amino Acid Sequences ◽  
Complement Factor ◽  
Factor B ◽  
Arginine Residues ◽  
Alternative Pathway Of Complement ◽  
Cnbr Cleavage

The alignment of all the CNBr-cleavage peptides of fragment Bb from human Factor B (a component of the alternative pathway of complement) was determined. This was derived from cleavage of the fragment Bb at arginine residues by using trypsin and clostripain. Details of the isolation and amino acid sequences of these peptides are given. Together with previously published N-terminal sequences of the CNBr-cleavage peptides [Christie & Gagnon (1982) Biochem. J. 201, 555-567], this provides the amino acid sequence of the N-terminal half of fragment Bb.

scholarly journals Triphenylmethane Reductase from Citrobacter sp. Strain KCTC 18061P: Purification, Characterization, Gene Cloning, and Overexpression of a Functional Protein in Escherichia coli

2005 ◽  
Vol 71 (12) ◽  
pp. 7955-7960 ◽  
Author(s):  
Moon-Sun Jang ◽  
Young-Mi Lee ◽  
Cheorl-Ho Kim ◽  
Jai-Heon Lee ◽  
Dong-Woo Kang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Enzymatic Reaction ◽  
Amino Acid Sequences ◽  
Binding Motif ◽  
Triphenylmethane Dyes ◽  
Functional Protein ◽  
Triphenylmethane Reductase

ABSTRACT We purified to homogeneity an enzyme from Citrobacter sp. strain KCTC 18061P capable of decolorizing triphenylmethane dyes. The native form of the enzyme was identified as a homodimer with a subunit molecular mass of about 31 kDa. It catalyzes the NADH-dependent reduction of triphenylmethane dyes, with remarkable substrate specificity related to dye structure. Maximal enzyme activity occurred at pH 9.0 and 60°C. The enzymatic reaction product of the triphenylmethane dye crystal violet was identified as its leuco form by UV-visible spectral changes and thin-layer chromatography. A gene encoding this enzyme was isolated based on its N-terminal and internal amino acid sequences. The nucleotide sequence of the gene has a single open reading frame encoding 287 amino acids with a predicted molecular mass of 30,954 Da. Although the deduced amino acid sequence displays 99% identity to the hypothetical protein from Listeria monocytogenes strain 4b H7858, it shows no overall functional similarity to any known protein in the public databases. At the N terminus, the amino acid sequence has high homology to sequences of NAD(P)H-dependent enzymes containing the dinucleotide-binding motif GXXGXXG. The enzyme was heterologously expressed in Escherichia coli, and the purified recombinant enzyme showed characteristics similar to those of the native enzyme. This is the first report of a triphenylmethane reductase characterized from any organism.

Ribosomal RNA: the message or matrix for ribosomal proteins

1976 ◽  
Vol 54 (2) ◽  
pp. 192-193
Author(s):  
D. R. Miller ◽  
A. T. Matheson ◽  
L. P. Visentin
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Ribosomal Protein ◽  
Ribosomal Rna ◽  
Ribosomal Proteins ◽  
Protein Sequences ◽  
Amino Acid Sequences ◽  
16S Ribosomal Rna ◽  
Degree Of Similarity

The known nucleotide sequence of Escherichia coli 16S ribosomal RNA has been converted to amino acid sequences in all possible ways, and compared to known ribosomal protein sequences. The degree of similarity is precisely what one would expect by chance alone, providing additional evidence that ribosomal proteins cannot be coded for by ribosomal RNA.

scholarly journals Characterization of a 12-Kilodalton Rhodanese Encoded byglpE of Escherichia coli and Its Interaction with Thioredoxin

2000 ◽  
Vol 182 (8) ◽  
pp. 2277-2284 ◽  
Author(s):  
W. Keith Ray ◽  
Gang Zeng ◽  
M. Benjamin Potters ◽  
Aqil M. Mansuri ◽  
Timothy J. Larson
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Amino Acid Sequences ◽  
E Coli ◽  
Active Site Cysteine ◽  
Clusters Of Orthologous Groups ◽  
Thioredoxin 1 ◽  
First Time

ABSTRACT Rhodaneses catalyze the transfer of the sulfane sulfur from thiosulfate or thiosulfonates to thiophilic acceptors such as cyanide and dithiols. In this work, we define for the first time the gene, and hence the amino acid sequence, of a 12-kDa rhodanese fromEscherichia coli. Well-characterized rhodaneses are comprised of two structurally similar ca. 15-kDa domains. Hence, it is thought that duplication of an ancestral rhodanese gene gave rise to the genes that encode the two-domain rhodaneses. The glpEgene, a member of the sn-glycerol 3-phosphate (glp) regulon of E. coli, encodes the 12-kDa rhodanese. As for other characterized rhodaneses, kinetic analysis revealed that catalysis by purified GlpE occurs by way of an enzyme-sulfur intermediate utilizing a double-displacement mechanism requiring an active-site cysteine. TheKm s for SSO3 2− and CN− were 78 and 17 mM, respectively. The apparent molecular mass of GlpE under nondenaturing conditions was 22.5 kDa, indicating that GlpE functions as a dimer. GlpE exhibited ak cat of 230 s−1. Thioredoxin 1 from E. coli, a small multifunctional dithiol protein, served as a sulfur acceptor substrate for GlpE with an apparentKm of 34 μM when thiosulfate was near itsKm , suggesting that thioredoxin 1 or related dithiol proteins could be physiological substrates for sulfurtransferases. The overall degree of amino acid sequence identity between GlpE and the active-site domain of mammalian rhodaneses is limited (∼17%). This work is significant because it begins to reveal the variation in amino acid sequences present in the sulfurtransferases. GlpE is the first among the 41 proteins in COG0607 (rhodanese-related sulfurtransferases) of the database Clusters of Orthologous Groups of proteins (http://www.ncbi.nlm.nih.gov/COG/ ) for which sulfurtransferase activity has been confirmed.

The Amino Acid Sequence of the N-Terminal Region of Some 30 S Ribosomal Proteins from Escherichia coli and Bacillus stearothermophilus: Homologies in Ribosomal Proteins

1973 ◽  
Vol 51 (8) ◽  
pp. 1215-1217 ◽  
Author(s):  
M. Yaguchi ◽  
C. Roy ◽  
A. T. Matheson ◽  
L. P. Visentin
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ribosomal Proteins ◽  
Bacillus Stearothermophilus ◽  
Terminal Region ◽  
Amino Terminal

The sequence of the amino terminal region of fifteen 30 S ribosomal proteins from Escherichia coli and three proteins from Bacillus stearothermophilus are compared.

Molecular Cloning, Nucleotide Sequence, and Expression in Escherichia coli of a Hemolytic Toxin (Aerolysin) Gene from Aeromonas trota

1998 ◽  
Vol 64 (7) ◽  
pp. 2473-2478 ◽  
Author(s):  
Ashraf A. Khan ◽  
Eungbin Kim ◽  
Carl E. Cerniglia
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Kanamycin Resistance ◽  
Aeromonas Salmonicida ◽  
Amino Acid Sequences ◽  
Nucleotide Sequence Data ◽  
Hemolytic Toxin

ABSTRACT Aeromonas trota AK2, which was derived from ATCC 49659 and produces the extracellular pore-forming hemolytic toxin aerolysin, was mutagenized with the transposon mini-Tn5Km1 to generate a hemolysin-deficient mutant, designated strain AK253. Southern blotting data indicated that an 8.7-kb NotI fragment of the genomic DNA of strain AK253 contained the kanamycin resistance gene of mini-Tn5Km1. The 8.7-kb NotI DNA fragment was cloned into the vector pGEM5Zf(−) by selecting for kanamycin resistance, and the resultant clone, pAK71, showed aerolysin activity in Escherichia coli JM109. The nucleotide sequence of the aerA gene, located on the 1.8-kbApaI-EcoRI fragment, was determined to consist of 1,479 bp and to have an ATG initiation codon and a TAA termination codon. An in vitro coupled transcription-translation analysis of the 1.8-kb region suggested that the aerA gene codes for a 54-kDa protein, in agreement with nucleotide sequence data. The deduced amino acid sequence of the aerA gene product ofA. trota exhibited 99% homology with the amino acid sequence of the aerA product of Aeromonas sobria AB3 and 57% homology with the amino acid sequences of the products of the aerA genes of Aeromonas salmonicida 17-2 and A. sobria 33.

scholarly journals Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli

1980 ◽  
Vol 187 (3) ◽  
pp. 905-908 ◽  
Author(s):  
G Hale ◽  
R N Perham
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Lipoic Acid ◽  
Pyruvate Dehydrogenase ◽  
Pyruvate Dehydrogenase Complex ◽  
Amino Acid Sequences ◽  
Single Amino Acid ◽  
Multienzyme Complex ◽  
Dehydrogenase Complex

Amino-acid sequences around two lipoic acid residues in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli were investigated. A single amino acid sequence of 13 residues was found. A repeated amino acid sequence in the lipoate acetyltransferase chain might explain this result.

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