Nucleotide sequences of the 2-oxoacid ferredoxin oxidoreductase and ferredoxin genes fromFrankiastrain EuIK1, a symbiont ofElaeagnus umbellataroot nodules

1999 ◽  
Vol 77 (9) ◽  
pp. 1279-1286
Author(s):  
Won Young Yoo ◽  
Si Bum Sung ◽  
Chung Sun An
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Genomic Library ◽  
Sequence Similarity ◽  
Root Nodules ◽  
Amino Acid Sequences ◽  
Elaeagnus Umbellata ◽  
Ferredoxin Oxidoreductase ◽  
B Subunit ◽  
A Subunit

A genomic clone, pEuNIFII, was isolated by screening a genomic library of Frankia strain EuIK1, a symbiont of Elaeagnus umbellata Thunb. root nodules. A 1.5-kb fragment of pEuNIF4.0, which contained ORF2 and N-terminal part of nifS, was used as a probe. A 7.2-kb BamHI fragment of pEuNIFII, which was proven to be adjacent to the probe, was subjected to sequence determination. The sequence analysis suggested one partial ORF followed by three open reading frames (ORFs). Two ORFs next to nifS encodes an a subunit (672 amino acids) and b subunit (347 amino acids) of a 2-oxoacid ferredoxin oxidoreducatase (OR), respectively. The third ORF encodes 114 amino acids of a 7Fe-type ferredoxin (Fdx). All ORFs are transcribed in the same direction as other nif genes. Alignment of the deduced amino acid sequences from frankiae OR revealed the motifs of gamma and alpha domains seen in other ORs in the a subunit, and the beta domain in the b subunit. Frankia or shows about 44% nucleotide sequence similarity with nifJ from Klebsiella pneumoniae, while frankiae fdx shows about 56% similarity with fdxI from Azotobacter vinelandii. These genes are reported for the first time in Frankia, and putative roles of their products in symbiosis is discussed in relation to nitrogen fixation and carbohydrate metabolism.Key words: 2-oxoacid ferredoxin oxidoreductase, ferredoxin, nucleotide sequence, Frankia EuIK1.

scholarly journals Nucleotide sequence, organization and characterization of the atp genes and the encoded subunits of Mycoplasma gallisepticum ATPase

1992 ◽  
Vol 285 (3) ◽  
pp. 881-888 ◽  
Author(s):  
O F Rasmussen ◽  
M H Shirvan ◽  
H Margalit ◽  
C Christiansen ◽  
S Rottem
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Close Association ◽  
Mycoplasma Gallisepticum ◽  
Amino Acid Sequences ◽  
Open Reading Frames ◽  
Alpha Helices ◽  
B Subunit ◽  
C Subunit ◽  
Delta Subunit

The nucleotide sequence of a 7.8 kbp DNA fragment from the genome of Mycoplasma gallisepticum has been determined. The fragment contains a cluster of nine tightly linked genes coding for the subunits of the M. gallisepticum ATPase. The gene order is I (I-subunit), B (a-subunit), E (c-subunit), F (b-subunit), H (delta-subunit), A (alpha-subunit), G (gamma-subunit), D (beta-subunit) and C (epsilon-subunit). Two open reading frames were identified in the flanking regions; one (ORFU), preceding the I gene, encodes at least 110 amino acids and the other (ORFS), following the C gene, encodes at least 90 amino acids. The deduced amino acid sequences of the various subunits are presented and discussed with regard to the structure, function and differing sensitivity of the M. gallisepticum enzyme to dicyclohexylcarbodiimide and aurovertin. The alpha- and beta-subunits of the F1 portion are well conserved (51% and 65% identity with those of Escherichia coli), whereas the gamma-, delta- and epsilon-subunits, as well as the F0-subunits, show a low percentage identity. Nonetheless, the secondary structure of the F0-subunits show a high degree of similarity to the corresponding subunits of E. coli. Two very strong potential amphipathic alpha-helices are predicted in the delta-subunit and the N-terminus of the b-subunit contains two hydrophobic helical stretches. The possible roles of these structural properties in the close association of the F1 and F0 multisubunit complexes among mycoplasmas are discussed.

Predicted structure of the bovine calcitonin gene-related peptide and the carboxy-terminal flanking peptide of bovine calcitonin precursor

1991 ◽  
Vol 6 (2) ◽  
pp. 147-152 ◽  
Author(s):  
K. Collyear ◽  
S. I. Girgis ◽  
G. Saunders ◽  
I. MacIntyre ◽  
G. Holt
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Genomic Library ◽  
Amino Acid Peptide ◽  
Related Peptide ◽  
Calcitonin Gene ◽  
Significant Homology ◽  
Human Counterpart ◽  
Carboxy Terminal

ABSTRACT We have isolated from a bovine genomic library a clone which contains the calcitonin (CT) and CT gene-related peptide (CGRP) sequences, using probes representing the human CT and CGRP sequences. Sequence analysis has identified the nucleotide sequence coding for bovine CT, its C-terminal flanking peptide and bovine CGRP. The deduced amino acid sequence of bovine CGRP revealed a significant homology with other CGRPs so far reported. It differs by only one amino acid from rat CGRPα and porcine CGRP, and by three and four amino acids from human CGRPβ and α respectively. Bovine CT has, however, only 14 out of 32 residues in common with human CT. As in the human CT precursor, the C-terminal flanking peptide of bovine CT precursor is a 21 amino acid peptide. It shares only 11 residues in common with its human counterpart. This study thus provides further evidence that CGRP, in contrast to CT and its C-terminal flanking peptide, is a highly conserved molecule.

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.

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.

ISOLATION AND CHARACTERIZATION OF THE GENES FOR THE a AND b SUBUNITS OF HUMAN COAGULATION FACTOR XIII

1987 ◽  
Author(s):  
A Ichinose ◽  
R E Bottenus ◽  
K R Loeb ◽  
E W Davie
Keyword(s):  
Amino Acid ◽  
Factor Xiii ◽  
Coagulation Factor ◽  
Amino Acid Sequences ◽  
Binding Region ◽  
Recombinant Phage ◽  
B Subunit ◽  
Isolation And Characterization ◽  
A Subunit ◽  
B Subunits

Factor XIII (plasma transglutaminase, fibrin stabilizing factor) is a plasma protein that plays an important role in the final stages of blood coagulation and fibrinolysis. The molecule occurs in blood as a tetramer (a2b2) consisting of two a. subunits and two b subunits. Recently, we have determined the amino acid sequences for both the a. and b subunits of human factor XIII by a combination of cDNA cloning and amino acid sequence analysis. cDNAs coding for the a (3.8 Kb) and b (2.2 Kb) subunits were used for the screening of human genomic DNA libraries. Among 12 × 106 recombinant phage, ∼30 have been shown to contain the sequences for the a subunit and ∼10 have been shown to contain the gene for the b subunit of factor XIII. The clones coding for the a. subunit span ∼90 Kb and have been characterized by restriction mapping. Southern blotting, and DNA sequencing. Both 5’ and 3’ ends of the genomic clones correspond to the 5’ and 3’portions of the cDNA for the a.subunit of factor XIII. The DNA sequence revealed that the activation peptide released ^thrombin (amino acid residues 137), the first putative Ca2+ binding region (around residue 251), the active Site Cys (amino acid residue 314), and the second putative Ca2+ binding region (around residue 473) are encoded by separate exons. Accordingly, the intervening sequences may separate the a subunit into functional and structural domains. The gene organization for the b subunit will also be presented. (Supported by NIH Grant HL 16919.)

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 Structure of a murine alpha interferon pseudogene with a repetitive R-type sequence in the 3' flanking region.

1985 ◽  
Vol 5 (6) ◽  
pp. 1343-1348 ◽  
Author(s):  
D Le Roscouet ◽  
G Vodjdani ◽  
Y Lemaigre-Dubreuil ◽  
M G Tovey ◽  
M Latta ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nucleotide Sequence ◽  
Genomic Library ◽  
Nucleotide Sequences ◽  
Alpha Interferon ◽  
Signal Sequences ◽  
Flanking Region ◽  
Flanking Regions ◽  
Mouse Genomic ◽  
Type Sequence

A murine alpha interferon pseudogene was identified in a mouse genomic library. The nucleotide sequence revealed several in-phase termination codons within the gene and repetitive oligonucleotides in the flanking regions. The nucleotide sequences and the amino acids of the peptide signal sequences were compared with known human alpha interferon genes and the pseudogene.

scholarly journals Essential Roles of Bdp1, a Subunit of RNA Polymerase III Initiation Factor TFIIIB, in Transcription and tRNA Processing

2002 ◽  
Vol 22 (10) ◽  
pp. 3264-3275 ◽  
Author(s):  
Akira Ishiguro ◽  
George A. Kassavetis ◽  
E. Peter Geiduschek
Keyword(s):  
Amino Acids ◽  
Rna Polymerase ◽  
Genomic Library ◽  
Rna Polymerase Iii ◽  
Rnase P ◽  
Initiation Factor ◽  
Physical Interaction ◽  
Polymerase Iii ◽  
A Subunit ◽  
Pol Iii

ABSTRACT The essential Saccharomyces cerevisiae gene BDP1 encodes a subunit of RNA polymerase III (Pol III) transcription factor (TFIIIB); TATA box binding protein (TBP) and Brf1 are the other subunits of this three-protein complex. Deletion analysis defined three segments of Bdp1 that are essential for viability. A central segment, comprising amino acids 327 to 353, was found to be dispensable, and cells making Bdp1 that was split within this segment, at amino acid 352, are viable. Suppression of bdp1 conditional viability by overexpressing SPT15 and BRF1 identified functional interactions of specific Bdp1 segments with TBP and Brf1, respectively. A Bdp1 deletion near essential segment I was synthetically lethal with overexpression of PCF1-1, a dominant gain-of-function mutation in the second tetracopeptide repeat motif (out of 11) of the Tfc4 (τ131) subunit of TFIIIC. The analysis also identifies a connection between Bdp1 and posttranscriptional processing of Pol III transcripts. Yeast genomic library screening identified RPR1 as the specific overexpression suppressor of very slow growth at 37°C due to deletion of Bdp1 amino acids 253 to 269. RPR1 RNA, a Pol III transcript, is the RNA subunit of RNase P, which trims pre-tRNA transcript 5′ ends. Maturation of tRNA was found to be aberrant in bdp1-Δ253-269 cells, and RPR1 transcription with the highly resolved Pol III transcription system in vitro was also diminished when recombinant Bdp1Δ253-269 replaced wild-type Bdp1. Physical interaction of RNase P with Bdp1 was demonstrated by coimmunoprecipitation and pull-down assays.

scholarly journals Cloning and nucleotide sequence of the gyrA gene from Campylobacter fetus subsp. fetus ATCC 27374 and characterization of ciprofloxacin-resistant laboratory and clinical isolates.

1997 ◽  
Vol 41 (3) ◽  
pp. 665-671 ◽  
Author(s):  
D E Taylor ◽  
A S Chau
Keyword(s):  
Nucleotide Sequence ◽  
Dna Gyrase ◽  
Amino Acid Identity ◽  
Gyra Gene ◽  
Reading Frame ◽  
B Subunit ◽  
Campylobacter Fetus ◽  
A Subunit ◽  
Fetus Subsp ◽  
Genomic Map

The gyrA gene of Campylobacter fetus subsp. fetus, which encodes the A subunit of DNA gyrase, was cloned, and its nucleotide sequence was determined. An open reading frame of 2,586 nucleotides which encodes a polypeptide of 862 amino acids with an Mr of 96,782 was identified. C. fetus subsp. fetus GyrA is most closely related to Campylobacter jejuni GyrA, with 73% homology at the nucleotide level and 78% identity between polypeptides. The next most closely related GyrA was that from Helicobacter pylori, with both DNA homology and amino acid identity of 63%. The gyrA and gyrB (DNA gyrase B subunit) genes were located on the genomic map of C. fetus subsp. fetus ATCC 27374 and shown to be separate. A clinical isolate of C. fetus subsp. fetus and a laboratory-derived mutant of ATCC 27374, both resistant to ciprofloxacin, had identical mutations within the quinolone resistance determining region. In both mutants a G-->T transversion, corresponding to a substitution of Asp-91 to Tyr in GyrA, was linked to ciprofloxacin resistance, giving MICs of 8 to 16 micrograms/ml.

scholarly journals Primary structure and domain organization of human alpha and beta adducin.

1991 ◽  
Vol 115 (3) ◽  
pp. 665-675 ◽  
Author(s):  
R Joshi ◽  
D M Gilligan ◽  
E Otto ◽  
T McLaughlin ◽  
V Bennett
Keyword(s):  
Amino Acids ◽  
Sequence Similarity ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Actin Binding ◽  
Cell Contact ◽  
Binding Motif ◽  
Rat Tissues ◽  
Erythroleukemia Cells ◽  
Skeletal Protein

Adducin is a membrane-skeletal protein which is a candidate to promote assembly of a spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. The complete sequence of both subunits of human adducin, alpha (737 amino acids), and beta (726 amino acids) has been deduced by analysis of the cDNAs. The two subunits have strikingly conserved amino acid sequences with 49% identity and 66% similarity, suggesting evolution by gene duplication. Each adducin subunit has three distinct domains: a 39-kD NH2-terminal globular protease-resistant domain, connected by a 9-kD domain to a 33-kD COOH-terminal protease-sensitive tail comprised almost entirely of hydrophilic amino acids. The tail is responsible for the high frictional ratio of adducin noted previously, and was visualized by EM. The head domains of both adducin subunits exhibit a limited sequence similarity with the NH2-terminal actin-binding motif present in members of the spectrin superfamily and actin gelation proteins. The COOH-termini of both subunits contain an identical, highly basic stretch of 22 amino acids with sequence similarity to the MARCKS protein. Predicted sites of phosphorylation by protein kinase C include the COOH-terminus and sites at the junction of the head and tail. Northern blot analysis of mRNA from rat tissues, K562 erythroleukemia cells and reticulocytes has shown that alpha adducin is expressed in all the tissues tested as a single message size of 4 kb. In contrast, beta adducin shows tissue specific variability in size of mRNA and level of expression. A striking divergence between alpha and beta mRNAs was noted in reticulocytes, where alpha adducin mRNA is present in at least 20-fold higher levels than that of beta adducin. The beta subunit thus is a candidate to perform a limiting role in assembly of functional adducin molecules.

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