scholarly journals Two genes encoding ‘minor’ legumin polypeptides in pea (Pisum sativum L.). Characterization and complete sequence of the LegJ gene

1988 ◽  
Vol 250 (1) ◽  
pp. 15-24 ◽  
Author(s):  
J A Gatehouse ◽  
D Bown ◽  
J Gilroy ◽  
M Levasseur ◽  
J Castleton ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Complete Sequence ◽  
Genomic Clone ◽  
Amino Acid Sequences ◽  
Flanking Sequence ◽  
Gene Encoding ◽  
Sequence Comparisons ◽  
Control Of Gene Expression ◽  
Pisum Sativum L ◽  
Genes Encoding

A genomic clone from pea (Pisum sativum L.) contains all of one gene encoding a ‘minor’ (B-type) legumin polypeptide, and most of a second very similar gene. The two genes, designated LegJ and LegK, are arranged in tandem, separated by approx. 6 kb. A complete sequence of gene LegJ and its flanking sequences is given, with as much of the sequence of gene LegK as is present on the genomic clone. Hybridization of 3′ flanking sequence probes to seed mRNA, and sequence comparisons with cDNA species, suggested that gene LegJ, and probably gene LegK, was expressed. The partial amino acid sequences of ‘minor’ legumin α- and beta-polypeptides were used to confirm the identity of these genes. The transciption start in gene LegJ was mapped. The 5′ flanking sequence of gene LegJ contains a sequence conserved in legumin genes from pea and other species, which is likely to have functional significance in control of gene expression. Sequence comparisons with legumin genes and cDNA species from Vicia faba and soya bean show that separation of legumin genes into A- and B-type subfamilies occurred before separation of the Viciae and Glycinae tribes.

scholarly journals The sequence of a gene encoding convicilin from pea (Pisum sativum L.) shows that convicilin differs from vicilin by an insertion near the N-terminus

1988 ◽  
Vol 251 (3) ◽  
pp. 717-726 ◽  
Author(s):  
D Bown ◽  
T H N Ellis ◽  
J A Gatehouse
Keyword(s):  
Amino Acid ◽  
Pisum Sativum ◽  
Seed Storage Protein ◽  
Promoter Sequence ◽  
Regulatory Elements ◽  
Flanking Sequence ◽  
Gene Encoding ◽  
Independent Events ◽  
Pisum Sativum L ◽  
N Terminus

The sequence of a gene encoding convicilin, a seed storage protein in pea (Pisum sativum L.), is reported. This gene, designated cvcA, is one of a sub-family of two active genes. The transcription start of cvcA was mapped. Convicilin genes are expressed in developing pea seed cotyledons, with maximum levels of the corresponding mRNA species present at 16-18 days after flowering. The gene sequence shows that convicilin is similar to vicilin, but differs by the insertion of a 121-amino-acid sequence near the N-terminus of the protein. This inserted sequence is very hydrophilic and has a high proportion of charged and acidic residues; it is of a similar amino acid composition to the sequences found near the C-terminal of the alpha-subunit in pea legumin genes, but is not directly homologous with them. Comparison of this sequence with the ‘inserted’ sequence in soya-bean (Glycine max) conglycinin (a homologous vicilin-type protein) suggests that the two insertions were independent events. The 5′ flanking sequence of the gene contains several putative regulatory elements, besides a consensus promoter sequence.

Direct cloning of genes encoding novel xylanases from the human gut

2005 ◽  
Vol 51 (3) ◽  
pp. 251-259 ◽  
Author(s):  
Hidenori Hayashi ◽  
Takashi Abe ◽  
Mitsuo Sakamoto ◽  
Hiroki Ohara ◽  
Toshimichi Ikemura ◽  
...  
Keyword(s):  
Intestinal Bacteria ◽  
Fecal Microbiota ◽  
Coli Strain ◽  
Amino Acid Sequences ◽  
Self Organizing Map ◽  
Human Gut ◽  
Gene Encoding ◽  
Genes Encoding ◽  
Ph Range ◽  
Self Organizing

The aim of this study was to identify a novel 1,4-β-xylanase gene from the mixed genome DNA of human fecal bacteria without bacterial cultivation. Total DNA was isolated from a population of bacteria extracted from fecal microbiota. Using PCR, the gene fragments encoding 5 different family 10 xylanases (xyn10A, xyn10B, xyn10C, xyn10D, and xyn10E) were found. Amino acid sequences deduced from these genes were highly homologous with those of xylanases from anaerobic intestinal bacteria such as Bacteroides spp. and Prevotella spp. Self-organizing map (SOM) analysis revealed that xynA10 was classified into Bacteroidetes. To confirm that one of these genes encodes an active enzyme, a full-length xyn10A gene was obtained using nested primers specific to the internal fragments and random primers. The xyn10A gene encoding the xylanase Xyn10A consists of 1146 bp and encodes a protein of 382 amino acids and a molecular weight of 43 552. Xyn10A was a single module novel xylanase. Xyn10A was purified from a recombinant Escherichia coli strain and characterized. This enzyme was optimally active at 40 °C and stable up to 50 °C at pH 6.5 and over the pH range 4.0–11.0 at 25 °C. In addition, 2 ORFs (ORF1 and ORF2) were identified upstream of xyn10A. These results suggested that many unidentified xylanolytic bacteria exist in the human gut and may contribute to the breakdown of xylan which contains dietary fiber.Key words: xylanase, human gut, fecal microbiota, phylogenetic analysis, self-organizing map.

scholarly journals Nuclear-Cytoplasmic Conflict in Pea (Pisum sativum L.) Is Associated with Nuclear and Plastidic Candidate Genes Encoding Acetyl-CoA Carboxylase Subunits

PLoS ONE ◽  
2015 ◽  
Vol 10 (3) ◽  
pp. e0119835 ◽  
Author(s):  
Vera S. Bogdanova ◽  
Olga O. Zaytseva ◽  
Anatoliy V. Mglinets ◽  
Natalia V. Shatskaya ◽  
Oleg E. Kosterin ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Candidate Genes ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Pisum Sativum L ◽  
Genes Encoding

scholarly journals DNA Methylation Patterns Differ between Free-Living Rhizobium leguminosarum RCAM1026 and Bacteroids Formed in Symbiosis with Pea (Pisum sativum L.)

2021 ◽  
Vol 9 (12) ◽  
pp. 2458
Author(s):  
Alexey M. Afonin ◽  
Emma S. Gribchenko ◽  
Evgeny A. Zorin ◽  
Anton S. Sulima ◽  
Vladimir A. Zhukov
Keyword(s):  
Pisum Sativum ◽  
Rhizobium Leguminosarum ◽  
Specific Pattern ◽  
Nitrogen Fixing ◽  
Free Living ◽  
Pisum Sativum L ◽  
Genome Methylation ◽  
Oxford Nanopore ◽  
Genes Encoding ◽  
Methylation Patterns

Rhizobium leguminosarum (Rl) is a common name for several genospecies of rhizobia able to form nitrogen-fixing nodules on the roots of pea (Pisum sativum L.) while undergoing terminal differentiation into a symbiotic form called bacteroids. In this work, we used Oxford Nanopore sequencing to analyze the genome methylation states of the free-living and differentiated forms of the Rl strain RCAM1026. The complete genome was assembled; no significant genome rearrangements between the cell forms were observed, but the relative abundances of replicons were different. GANTC, GGCGCC, and GATC methylated motifs were found in the genome, along with genes encoding methyltransferases with matching predicted target motifs. The GGCGCC motif was completely methylated in both states, with two restriction–modification clusters on different replicons enforcing this specific pattern of methylation. Methylation patterns for the GANTC and GATC motifs differed significantly depending on the cell state, which indicates their possible connection to the regulation of symbiotic differentiation. Further investigation into the differences of methylation patterns in the bacterial genomes coupled with gene expression analysis is needed to elucidate the function of bacterial epigenetic regulation in nitrogen-fixing symbiosis.

scholarly journals Regulation of storage-protein synthesis in pea (Pisum sativum L.) cotyledons under conditions of sulphur deficiency

1985 ◽  
Vol 232 (1) ◽  
pp. 261-265 ◽  
Author(s):  
I M Evans ◽  
J A Gatehouse ◽  
D Boulter
Keyword(s):  
Gene Expression ◽  
Pisum Sativum ◽  
Gene Transcription ◽  
Storage Protein ◽  
Control Of Gene Expression ◽  
Sulphur Deficiency ◽  
Pisum Sativum L ◽  
S Deficiency ◽  
Vicilin Gene ◽  
Storage Protein Genes

The effects of sulphur deficiency on the expression of storage-protein genes in developing pea (Pisum sativum) cotyledons were studied. Legumin-gene transcription was decreased by S-deficiency, but not to the same extent as the decrease in the level of legumin mRNA. Vicilin-gene transcription was not significantly affected. Control of gene expression may thus occur during transcription and/or post-transcriptional events.

The Bacillus subtilisNucleotidyltransferase Is a tRNA CCA-Adding Enzyme

1998 ◽  
Vol 180 (23) ◽  
pp. 6276-6282 ◽  
Author(s):  
Lelia C. Raynal ◽  
Henry M. Krisch ◽  
Agamemnon J. Carpousis
Keyword(s):  
Purple Bacteria ◽  
Rna Degradation ◽  
Gene Encoding ◽  
Sequence Comparisons ◽  
Gram Negative ◽  
E Coli ◽  
Gram Positive Bacteria ◽  
Genes Encoding ◽  
Gram Negative Organisms ◽  
Polymerase I

ABSTRACT There has been increased interest in bacterial polyadenylation with the recent demonstration that 3′ poly(A) tails are involved in RNA degradation. Poly(A) polymerase I (PAP I) of Escherichia coli is a member of the nucleotidyltransferase (Ntr) family that includes the functionally related tRNA CCA-adding enzymes. Thirty members of the Ntr family were detected in a search of the current database of eubacterial genomic sequences. Gram-negative organisms from the β and γ subdivisions of the purple bacteria have two genes encoding putative Ntr proteins, and it was possible to predict their activities as either PAP or CCA adding by sequence comparisons with theE. coli homologues. Prediction of the functions of proteins encoded by the genes from more distantly related bacteria was not reliable. The Bacillus subtilis papS gene encodes a protein that was predicted to have PAP activity. We have overexpressed and characterized this protein, demonstrating that it is a tRNA nucleotidyltransferase. We suggest that the papS gene should be renamed cca, following the notation for itsE. coli counterpart. The available evidence indicates thatcca is the only gene encoding an Ntr protein, despite previous suggestions that B. subtilis has a PAP similar toE. coli PAP I. Thus, the activity involved in RNA 3′ polyadenylation in the gram-positive bacteria apparently resides in an enzyme distinct from its counterpart in gram-negative bacteria.

Structure and sequence of a mouse gene encoding an androgen-regulated protein: a new member of the seminal vesicle secretory protein family

1995 ◽  
Vol 15 (3) ◽  
pp. 305-316 ◽  
Author(s):  
A M Simon ◽  
G Veyssière ◽  
Cl Jean
Keyword(s):  
Seminal Vesicle ◽  
Genomic Library ◽  
Protein A ◽  
Cdna Probe ◽  
Secretory Protein ◽  
Complete Sequence ◽  
Start Codon ◽  
Regulatory Sequences ◽  
Gene Encoding ◽  
Sequence Comparisons

ABSTRACT The gene encoding MSVSP99 (mouse seminal vesicle secretory protein of 99 amino acids), an androgen-dependent protein specifically expressed in the mouse seminal vesicle, was isolated and sequenced. A mouse genomic library constructed in the λEMBL12 vector was screened using a full length cDNA probe. One genomic clone was selected, 7·4 kb of which were shown to contain the whole MSVSP99 gene. The complete sequence of the MSVSP99 gene (1·7 kb), plus 0·8 and 0·3 kb of the 5′ and 3′ flanking regions respectively, has been determined. The gene is composed of four exons interrupted by three introns. The size range for the four exons is 47–217 bp, while that of introns is 87–615 bp. The transcription start site was identified as an adenine residue located 21 nucleotides upstream from the ATG start codon. Putative TATA and CAAT boxes were identified, along with a number of regions that shared homologies with known regulatory sequences. These included androgen-responsive elements located in the promoter as well as in the gene sequence. Sequence comparisons with other androgen-responsive genes showed strong homologies between the MSVSP99 gene and the seminal vesicle secretory protein (SVS) family genes (rat SVS II, IV, V and VI). Moreover, some regions were found to be conserved between the MSVSP99 gene and the human semenogelin I and II genes.

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