scholarly journals Structural gene and complete amino acid sequence of Vibrio alginolyticus collagenase

1992 ◽  
Vol 281 (3) ◽  
pp. 703-708 ◽  
Author(s):  
H Takeuchi ◽  
Y Shibano ◽  
K Morihara ◽  
J Fukushima ◽  
S Inami ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Structural Gene ◽  
Sequence Similarity ◽  
Vibrio Alginolyticus ◽  
Amino Acid Sequences ◽  
Dna Encoding ◽  
Cloned Gene ◽  
Collagenase Gene

The DNA encoding the collagenase of Vibrio alginolyticus was cloned, and its complete nucleotide sequence was determined. When the cloned gene was ligated to pUC18, the Escherichia coli expression vector, bacteria carrying the gene exhibited both collagenase antigen and collagenase activity. The open reading frame from the ATG initiation codon was 2442 bp in length for the collagenase structural gene. The amino acid sequence, deduced from the nucleotide sequence, revealed that the mature collagenase consists of 739 amino acids with an Mr of 81875. The amino acid sequences of 20 polypeptide fragments were completely identical with the deduced amino acid sequences of the collagenase gene. The amino acid composition predicted from the DNA sequence was similar to the chemically determined composition of purified collagenase reported previously. The analyses of both the DNA and amino acid sequences of the collagenase gene were rigorously performed, but we could not detect any significant sequence similarity to other collagenases.

scholarly journals Nucleotide and derived amino acid sequences of a cDNA coding for pre-uteroglobin from the lung of the hare (Lepus capensis)

1986 ◽  
Vol 235 (3) ◽  
pp. 895-898 ◽  
Author(s):  
M S López de Haro ◽  
A Nieto
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Untranslated Regions ◽  
Coding Region ◽  
Homologous Proteins ◽  
Lepus Capensis ◽  
Rabbit Gene

An almost full-length cDNA coding for pre-uteroglobin from hare lung was cloned and sequenced. The derived amino acid sequence indicated that hare pre-uteroglobin contained 91 amino acids, including a signal peptide of 21 residues. Comparison of the nucleotide sequence of hare pre-uteroglobin cDNA with that previously reported for the rabbit gene indicated five silent point substitutions and six others leading to amino acid changes in the coding region. The untranslated regions of both pre-uteroglobin mRNAs were very similar. The amino acid changes observed are discussed in relation to the different progesterone-binding abilities of both homologous proteins.

Molecular Heterogeneity of the L-1 Metallo-β-Lactamase Family from Stenotrophomonas maltophilia

1998 ◽  
Vol 42 (5) ◽  
pp. 1245-1248 ◽  
Author(s):  
François Sanschagrin ◽  
Julien Dufresne ◽  
Roger C. Levesque
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Stenotrophomonas Maltophilia ◽  
Amino Acid Sequences ◽  
Molecular Heterogeneity ◽  
Gene Encoding ◽  
Class B

ABSTRACT We have determined the nucleotide sequence of the blaSgene encoding the carbapenem-hydrolyzing L-1 β-lactamase fromStenotrophomonas maltophilia GN12873. Analysis of the DNA and deduced amino acid sequences identified a product of 290 amino acids. Comparisons of the L-1 amino acid sequence with those of other zinc β-lactamases showed 88.6% identity with the L-1 enzyme fromS. maltophilia IID1275 and less than 20% identity with other class B metalloenzymes.

scholarly journals Amino acid sequence of alpha-amylase from Bacillus amyloliquefaciens deduced from the nucleotide sequence of the cloned gene.

1983 ◽  
Vol 258 (2) ◽  
pp. 1007-1013 ◽  
Author(s):  
K Takkinen ◽  
R F Pettersson ◽  
N Kalkkinen ◽  
I Palva ◽  
H Söderlund ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Bacillus Amyloliquefaciens ◽  
Alpha Amylase ◽  
Cloned Gene

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 of the L-lactate dehydrogenase of Bacillus caldotenax deduced from the nucleotide sequence of the cloned gene

1987 ◽  
Vol 165 (3) ◽  
pp. 581-586 ◽  
Author(s):  
David A. BARSTOW ◽  
Jonathan P. MURPHY ◽  
Andy F. SHARMAN ◽  
Anthony R. CLARKE ◽  
J. John HOLBROOK ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lactate Dehydrogenase ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Cloned Gene

scholarly journals Molecular biology of the 2-haloacid halidohydrolase IVa from Pseudomonas cepacia MBA4

1992 ◽  
Vol 284 (1) ◽  
pp. 87-93 ◽  
Author(s):  
U Murdiyatmo ◽  
W Asmara ◽  
J S H Tsang ◽  
A J Baines ◽  
A T Bull ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Structural Gene ◽  
Sequence Data ◽  
Structural Data ◽  
Amino Acid Sequences ◽  
Open Reading Frames ◽  
Pseudomonas Cepacia ◽  
Chromosomal Dna ◽  
High Level

The structural gene (hdl IVa) for the Pseudomonas cepacia MBA4 2-haloacid halidohydrolase IVa (Hdl IVa) was isolated on a 1.6 kb fragment of Ps. cepacia MBA4 chromosomal DNA. The recombinant halidohydrolase was expressed in Escherichia coli and Pseudomonas putida and the structural gene was subcloned on to the tac expression vector pBTac1. High-level expression from the tac promoter was seen to be temperature-dependent, a consequence of the nucleotide sequence adjacent to the fragment encoding the halidohydrolase. The nucleotide sequence of the fragment encoding the Hdl IVa was determined and analysed. Three ATG codons were identified in one of the open reading frames and the one corresponding to the start of the hdl IVa structural gene was determined by comparison of the predicted amino acid sequences with the experimentally determined N-terminal sequences of halidohydrolase IVa. The hdl IVa gene encoded a 231-amino acid-residue protein of M(r) 25,900. The sequence and predicted structural data are discussed and comparison is made with sequence data for other halidohydrolases.

Sequence analysis and expression patterns of two nifA genes from Frankia EuIK1

2001 ◽  
Vol 28 (9) ◽  
pp. 939
Author(s):  
Hyoungseok Lee ◽  
Si Bum Sung ◽  
Ho Bang Kim ◽  
Chung Sun An
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Nitrogenase Activity ◽  
Sequence Similarity ◽  
Expression Patterns ◽  
Amino Acid Sequences ◽  
Start Codon ◽  
Nodule Development ◽  
Intergenic Sequence ◽  
Elaeagnus Umbellata

This paper originates from an address at the 8th International Symposium on Nitrogen Fixation with Non-Legumes, Sydney, NSW, December 2000 Two nifA genes were cloned from Frankia EuIK1 strain, a symbiont of Elaeagnus umbellata Thunb. and analysed on the basis of their deduced amino acid sequences and expression patterns. The complete nucleotide sequence of 1926 bp of nifA1 and 1524 bp of nifA2 was determined, respectively. A putative NifA-binding site was found –95 to about –80 bp upstream of start codon for nifA1 ORF as TGT-N10-ACA, but the clpB ORF was followed by nifA2 ORF with 15 bp of intergenic sequence. Deduced amino acid sequence showed that two nifA genes encode typical NifA, having three major domains and two linkers, and their central domains of NifA1 and NifA2 showed sequence similarity of 70–75% with those from other NifA proteins. However, entire NifA2 ORF is more similar to alternative NifA (60%) than to typical NifA (53%). Conserved amino acid sequence in helix-turn-helix motif of typical NifA was also found in NifA1, but it was not conserved in NifA2, which is also common in alternative NifA proteins. Moreover, the expression of nifA1 during nodule development was similar to that of Rhizobium meliloti in that it was expressed at low level constitutively, while that of nifA2 was similar to the pattern of nifH, structural gene for nitrogenase reductase, in that its transcripts level was changed in accordance with nitrogenase activity. These results indicate that nifA1 and nifA2 might be classified into typical nifA and alternative nifA, respectively. This is the first report on the presence of two nifA genes in Frankia.

scholarly journals Genomic organization of infectious salmon anaemia virus

2002 ◽  
Vol 83 (2) ◽  
pp. 421-428 ◽  
Author(s):  
Sharon C. Clouthier ◽  
Trent Rector ◽  
Nathan E. C. Brown ◽  
Eric D. Anderson
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Signal Sequence ◽  
Amino Acid Sequences ◽  
Surface Glycoprotein ◽  
Predicted Amino Acid Sequence ◽  
Infectious Salmon Anaemia Virus ◽  
Virion Protein ◽  
Infectious Salmon Anaemia

The RNA genome segment order, nucleotide sequence and the putative encoded proteins were determined for infectious salmon anaemia virus (ISAV). Eight segments of genomic viral RNA between 1·0 and 2·4 kb in length were identified. RNA segments 1–6 each had a predicted single open reading frame encoding the P1, PB1, NP, P2, P3 and HA proteins, respectively. Segment 7 encoded the P4/P5 proteins and segment 8 encoded the P6/P7 proteins. Seven virion proteins with molecular masses between 25 and 72 kDa were found by SDS–PAGE analysis. The 72 and 42 kDa proteins were immunoreactive with ISAV antiserum from Atlantic salmon. The molecular mass of the 72 kDa virion protein suggested that it was the NP protein encoded by segment 3. The amino acid sequence was conserved, sharing 96·6% identity with the NP protein of a Scottish ISAV isolate. Comparison of the amino acid sequences obtained by N-terminal analyses and cDNA nucleotide translation revealed that the 42 and 47 kDa proteins were the HA and P3 proteins encoded by segments 6 and 5, respectively. In addition, analysis provided evidence for their protein synthesis initiation sites. Like the HA protein, the signal sequence and potential glycosylation sites of P3 suggested that it was a surface glycoprotein. The predicted amino acid sequence shared 83·1, 84·0 and 99·6% identity to the predicted P3 protein sequences for ISAV isolates from Norway, Scotland and Maine, respectively. These results establish the specificity, migration, number and nucleotide sequence of the eight RNA segments of the ISAV genome.

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