Nucleotide and deduced amino acid sequences of an alkaline pullulanase from the alkaliphilic bacterium Bacillus sp. KSM-1876 1The nucleotide sequence data have been submitted to the DDBJ, GenBank, and EMBL data banks under accession No. AB049812. 1

2001 ◽  
Vol 1545 (1-2) ◽  
pp. 367-371 ◽  
Author(s):  
Yuji Hatada ◽  
Kazuhiro Saito ◽  
Hiroshi Hagihara ◽  
Katsuya Ozaki ◽  
Susumu Ito
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Sequence Data ◽  
Amino Acid Sequences ◽  
Bacillus Sp ◽  
Nucleotide Sequence Data ◽  
Bacterium Bacillus ◽  
Alkaliphilic Bacterium ◽  
Data Banks

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.

Expression patterns of the genes that encode lectin or lectin-related polypeptides in Robinia pseudoacacia

1999 ◽  
Vol 26 (5) ◽  
pp. 495 ◽  
Author(s):  
Kazumasa Yoshida ◽  
Kiyoshi Tazaki
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Sequence Data ◽  
Expression Patterns ◽  
Robinia Pseudoacacia ◽  
Regulation Of Expression ◽  
Nucleotide Sequence Data ◽  
Reading Frame ◽  
Inner Bark

Three genomic clones (Rplec2, Rplec5 and Rplec6) and a cDNA clone (LECRPA4) that encoded lectin or lectin-related polypeptides were isolated from Robinia pseudoacacia L. A comparison of the nucleotide sequences of Rplec2 and a previously reported cDNA for the subunit indicated that Rplec2 encoded the 29 kDa subunit of the inner-bark lectin RPbAI. Rplec5 encoded a polypeptide whose deduced amino acid sequence was 96.1% identical to that of a subunit of seed lectin. The amino acid sequence deduced from the open reading frame of Rplec6 showed 61.1% identity to that encoded by Rplec5. LECRPA4 was isolated from an inner bark cDNA library and appeared to encode the 26 kDa subunit of inner-bark lectin RPbAII. The expression patterns of the various genes in tissues were examined by the reverse transcriptase-polymerase chain reaction (RT-PCR) with appropriate primers. Rplec2 transcripts were detected in the inner bark and roots. Rplec5 transcripts were detected in the inner bark, seeds and roots. No Rplec6 transcripts were detected in all tissues examined. LECRPA4 transcripts were found in leaves and in the inner bark. The level of expression of Rplec2 in the inner bark appeared to be similar in samples collected in different years and from different trees, whereas levels of expression of Rplec5 and LECRPA4 varied. These results suggest the differential regulation of expression of members of the lectin gene family in tissues of R. pseudoacacia. The nucleotide sequence data reported herein will appear in the DDBJ, EMBL and GenBank Nucleotide Sequence Databases under the accession numbers AB 012632 (Rplec2), AB012633 (Rplec5), AB012634 (Rplec6) and AB012635 (LECRPA4).

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.

scholarly journals Sequence, catalytic properties and expression of chicken glutathione-dependent prostaglandin D2 synthase, a novel class Sigma glutathione S-transferase

1998 ◽  
Vol 333 (2) ◽  
pp. 317-325 ◽  
Author(s):  
Anne M. THOMSON ◽  
David J. MEYER ◽  
John D. HAYES
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Expressed Sequence Tag ◽  
Sequence Data ◽  
Cdna Clones ◽  
Prostaglandin D2 ◽  
Glutathione S Transferase ◽  
Nucleotide Sequence Data ◽  
Chicken Spleen ◽  
Wide Range

The Expressed Sequence Tag database has been screened for cDNA clones encoding prostaglandin D2 synthases (PGDSs) by using a BLAST search with the N-terminal amino acid sequence of rat GSH-dependent PGDS, a class Sigma glutathione S-transferase (GST). This resulted in the identification of a cDNA from chicken spleen containing an insert of approx. 950 bp that encodes a protein of 199 amino acid residues with a predicted molecular mass of 22732 Da. The deduced primary structure of the chicken protein was not only found to possess 70% sequence identity with rat PGDS but it also demonstrated more than 35% identity with class Sigma GSTs from a range of invertebrates. The open reading frame of the chicken cDNA was expressed in Escherichia coli and the purified protein was found to display high PGDS activity. It also catalysed the conjugation of glutathione with a wide range of aryl halides, organic isothiocyanates and α,β-unsaturated carbonyls, and exhibited glutathione peroxidase activity towards cumene hydroperoxide. Like other GSTs, chicken PGDS was found to be inhibited by non-substrate ligands such as Cibacron Blue, haematin and organotin compounds. Western blotting experiments showed that among the organs studied, the expression of PGDS in the female chicken is highest in liver, kidney and intestine, with only small amounts of the enzyme being found in chicken spleen; in contrast, the rat has highest levels of PGDS in the spleen. Collectively, these results show that the structure and function, but not the expression, of the GSH-requiring PGDS is conserved between chicken and rat. The nucleotide sequence data reported in this paper have been submitted to the EMBL, GenBank, GSDB and DDBJ Nucleotide Sequence Databases under the accession number AJ006405.

scholarly journals A novel giant secretion polypeptide in Chironomus salivary glands: implications for another Balbiani ring gene.

1985 ◽  
Vol 101 (3) ◽  
pp. 1044-1051 ◽  
Author(s):  
W Y Kao ◽  
S T Case
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Salivary Glands ◽  
Cyanogen Bromide ◽  
Tryptic Peptide ◽  
Amino Acid Sequences ◽  
The Other ◽  
Balbiani Ring ◽  
Sequence Organization ◽  
Peptide Maps

Chironomus salivary glands contain a family of high Mr (approximately 1,000 X 10(3)) secretion polypeptides thought to consist of three components: sp-Ia, sp-Ib, and sp-Ic. The use of a new extraction protocol revealed a novel high Mr component, sp-Id. Results of a survey of individual salivary glands indicated that sp-Id was widespread in more than a dozen strains of C. tentans and C. pallidivittatus. Sp-Id was phosphorylated at Ser residues, and a comparison of cyanogen bromide and tryptic peptide maps of 32P-labeled polypeptides suggested that sp-Ia, sp-Ib, and sp-Id are comprised of similar but nonidentical tandemly repeated amino acid sequences. We concluded that sp-Id is encoded by an mRNA whose size and nucleotide sequence organization are similar to Balbiani ring (BR) mRNAs that code for the other sp-I components. Furthermore, parallel repression of sp-Ib and sp-Id synthesis by galactose led us to hypothesize that both of their genes exist within Balbiani ring 2.

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