scholarly journals Characterization and In Silico Analysis of Pregnancy-Associated Glycoprotein-1 Gene of Buffalo (Bubalus bubalis)

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Jerome A. ◽  
S. K. Singh ◽  
S. K. Agarwal ◽  
Mohini Saini ◽  
Ashwin Raut
Keyword(s):  
Amino Acids ◽  
Mammalian Species ◽  
Evolutionary Relationship ◽  
In Silico Analysis ◽  
Bubalus Bubalis ◽  
Phylogenetic Study ◽  
Base Pairs ◽  
Reading Frame ◽  
Genes Encoding ◽  
Amino Acid Signal Peptide

Pregnancy-Associated Glycoproteins (PAGs) are trophoblastic proteins belonging to the Aspartic proteinase family secreted by different placental cells of many mammalian species. They play a pivotal role in placentogenesis, foetomaternal unit remodeling, and implantation. The identification of the genes encoding those proteins will be helpful to unravel the intricate embryogenomic functions during pregnancy establishment. Considering importance of these proteins, the present study was undertaken to characterize the pregnancy associated glycoprotein-1 gene of buffalo. An 1181 base pairs buffalo Pregnancy-Associated Glycoprotein PAG-1 gene was PCR amplified from the RNA obtained from the fetal cotyledons. BLAST analysis of the buffalo PAG-1 sequence retrieved a total of 20 cattle, 5 goat, and 4 sheep PAG sequences, exhibiting more than 80% similarity. Buffalo PAG-1 gene contained an uninterrupted open reading frame of 1140 base pairs encoding 380 amino acids that possess a 15 amino acid signal peptide and mature peptide of 365 amino acids. The phylogenetic study of the buffalo PAG-1 gene revealed buffalo PAG-1 is more related to cattle, goat, and sheep PAG-1 sequences. By this study characterization of buffalo PAG-1 gene and its evolutionary relationship was deduced for the first time.

Three new components contained in the vitelline coat of Tegula pfeifferi

Zygote ◽  
1999 ◽  
Vol 8 (S1) ◽  
pp. S61-S61 ◽  
Author(s):  
Kazu Haino-Fukushima ◽  
Xuxi Fan ◽  
Shouka Nakamura
Keyword(s):  
Amino Acids ◽  
Polyacrylamide Gel Electrophoresis ◽  
Enzymatic Reaction ◽  
Base Pairs ◽  
Sulphated Polysaccharides ◽  
Reading Frame ◽  
Glycosylation Sites ◽  
Long Time ◽  
Protein Components ◽  
Vitelline Coat

The vitelline coat (VC) lysin of Tegula, a marine molluscan genus, is released from the acrosome of sperm during fertilisation and can lyse the VC of only the same species. The lytic action of this lysin against the VC is not an enzymatic reaction, but a stoichiometric and irreversible one (Haino-Fukushima, 1974).The VC of Tegula pfeifferi consists of glycoproteins containing sulphated polysaccharides, which account for roughly two-thirds of the entire weight of the VC. The presence of a large quantity of polysaccharides in the VC had prevented rapid progress in the analysis of its protein components. Last year, we succeeded in a complete solubilisation of the VC by boiling for a long time in 1% SDS solution, and determined the cDNA sequence coding for a mature 41 kDa glycoprotein, which appears to be the major component of the VC from the results of SDS-polyacrylamide gel electrophoresis (PAGE). The cDNA, referred to as vcp41, comprises 1072 base pairs and contains one open reading frame with a sequence for 319 amino acids containing 19 amino acids of a signal peptide. The deduced amino acid sequence has five N-glycosylation sites and ten cysteine residues. It seems that almost 7 kDa in this 41kDa glycoprotein is polysaccharide constituents (Fan & Haino-Fukushima, 1998).

scholarly journals Sequencing and expression analysis of hepcidin mRNA in donkey (Equus asinus) liver

2012 ◽  
Vol 32 (10) ◽  
pp. 1050-1054 ◽  
Author(s):  
José P. Oliveira-Filho ◽  
Jessica A. Marques ◽  
Paulo Henrique J. Cunha ◽  
Gildenor X. Medeiros ◽  
Franklin Riet-Correa ◽  
...  
Keyword(s):  
Amino Acids ◽  
Iron Metabolism ◽  
Acute Inflammation ◽  
Mammalian Species ◽  
Reading Frame ◽  
Equus Asinus ◽  
Reference Gene Expression ◽  
Inflammatory Processes ◽  
Sequencing And Expression ◽  
Hepcidin Mrna

The hypoferremia that is observed during systemic inflammatory processes is mediated by hepcidin, which is a peptide that is mainly synthesized in the livers of several mammalian species. Hepcidin plays a key role in iron metabolism and in the innate immune system. It's up-regulation is particularly useful during acute inflammation, and it restricts the iron availability that is necessary for the growth of pathogenic microorganisms. In this study, the hepcidin mRNA of Equus asinus has been characterized, and the expression of donkey hepcidin in the liver has been determined. The donkey hepcidin sequence has an open reading frame (ORF) of 261 nucleotides, and the deduced corresponding protein sequence has 86 amino acids. The amino acid sequence of donkey hepcidin was most homologous to Equus caballus (98%). The mature donkey hepcidin sequence (25 amino acids) was 100% homologous to the equine mature hepcidin and has eight conserved cysteine residues that are found in all of the investigated hepcidin sequences. The expression profile of donkey hepcidin in the liver was high and was similar to the reference gene expression. The donkey hepcidin sequence was deposited in GenBankTM (HQ902884) and may be useful for additional studies on iron metabolism and the inflammatory process in this species.

The in Silicon Cloning ILF2 Gene and Prediction of ILF2 Protein Structure in Sheep

2011 ◽  
Vol 345 ◽  
pp. 423-428
Author(s):  
Ying Ning Sun ◽  
Yu Zhao ◽  
Wei Yu Wang
Keyword(s):  
Amino Acids ◽  
Gene Sequence ◽  
Rna Binding ◽  
Binding Domain ◽  
Nucleic Acid Binding ◽  
Zebra Fish ◽  
Probe Sequence ◽  
Base Pairs ◽  
Reading Frame ◽  
Cloned Cdna

In silicon cloning, we obtained ILF2 gene by using human ILF2 gene sequence (NM_004515) to be probe. Sequence analysis showed that the in silicon cloned cDNA was 1662 base pairs long with an open reading frame (ORF) containing 1173 nucleotides encoding a protein of 390 amino acids. 5’-untranslated region (UTR) was 74 bp, and 3’-UTR was 413 bp. A comparison of the sheep ILF2 with cow, horse, human, mouse, xenopus and zebra fish ILF2 amino acids had 96%, 91%, 91%, 81%, 61%, and 54% identity. The PI was 5.19, and molecular weight of the deduced protein was 43 050.12 Da. The pig ILF2 contained a RGG-rich single-stranded RNA-binding domain and a DZF zinc-finger nucleic acid binding domain. This study laid a foundation for further analysis of structure, expression and regulation of ILF2 gene in sheep.

scholarly journals The Presence of Diverse IS Elements and an avrPphD Homologue That Acts as a Virulence Factor on the Pathogenicity Plasmid of Erwinia herbicola pv. gypsophilae

2002 ◽  
Vol 15 (7) ◽  
pp. 709-716 ◽  
Author(s):  
Ming Guo ◽  
Shulamit Manulis ◽  
Henia Mor ◽  
Isaac Barash
Keyword(s):  
Amino Acids ◽  
Pseudomonas Syringae ◽  
Upstream Region ◽  
Erwinia Herbicola ◽  
High Identity ◽  
Reading Frame ◽  
Type Iii Effectors ◽  
Is Elements ◽  
Genes Encoding ◽  
Indole 3 Acetic Acid

The pathogenicity of Erwinia herbicola pv. gypsophilae (Ehg) and Erwinia herbicola pv. betae (Ehb) is dependent on a native plasmid (pPATHEhg or pPATHEhb) that harbors the hrp gene cluster, genes encoding type III effectors, phytohormones, biosynthetic genes, and several copies of IS1327. Sequence analysis of the hrp-flanking region in pPATHEhg (cosmid pLA150) revealed a cluster of four additional IS elements designated as ISEhe1, ISEhe2, ISEhe3, and ISEhe4. Two copies of another IS element (ISEhe5) were identified on the upstream region of the indole-3-acetic acid operon located on the same cosmid. Based on homology of amino acids and genetic organization, ISEhe1 belongs to the IS630 family, ISEhe2 to the IS5 family, ISEhe3 and ISEhe4 to different groups of the IS3 family, and ISEhe5 to the IS1 family. With the exception of ISEhe4, one to three copies of all the other IS elements were identified only in pathogenic strains of Erwinia herbicola pv. gypsophilae and Erwinia herbicola pv. betae whereas ISEhe4 was present in both pathogenic and nonpathogenic strains. An open reading frame that exhibited high identity (89% in amino acids) to AvrPphD of Pseudomonas syringae pv. phaseolicola was present within the cluster of IS elements. An insertional mutation in the AvrPphD Ehg reduced gall size in gypsophila by approximately 85%. In addition, remnants of known genes from four different bacteria were detected on the same cosmid.

scholarly journals Phospholipase Cζ, the trigger of egg activation in mammals, is present in a non-mammalian species

Reproduction ◽  
2005 ◽  
Vol 130 (2) ◽  
pp. 157-163 ◽  
Author(s):  
K Coward ◽  
C P Ponting ◽  
H-Y Chang ◽  
O Hibbitt ◽  
P Savolainen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Phospholipase C ◽  
Functional Properties ◽  
Mammalian Species ◽  
Open Reading Frame ◽  
Domestic Chicken ◽  
Egg Activation ◽  
Specific Gene ◽  
Reading Frame ◽  
First Time

The activation of the egg to begin development into an embryo is triggered by a sperm-induced increase in intracellular egg Ca2+. There has been much controversy about how the sperm induces this fundamental developmental event, but recent studies suggest that, in mammals, egg activation is triggered by a testis-specific phospholipase C: PLCζ. Since the discovery of PLCζ, it has been unclear whether its role in triggering egg activation is common to all vertebrates, or is confined to mammals. Here, we demonstrate for the first time that PLCζ is present in a non-mammalian vertebrate. Using genomic and cDNA databases, we have identified the cDNA encoding a PLCζ orthologue in the domestic chicken that, like the mammalian isoforms, is a testis-specific gene. The chicken PLCζ cDNA is 2152 bp in size and encodes an open reading frame of 639 amino acids. When injected into mouse oocytes, chicken PLCζ cRNA triggers Ca2+ oscillations, indicating that it has functional properties similar to those of mammalian PLCζ. Our findings suggest that PLCζ may have a universal role in triggering egg activation in vertebrates.

A comparison of GABAC and ρ subunit receptors from the white perch retina

1997 ◽  
Vol 14 (5) ◽  
pp. 843-851 ◽  
Author(s):  
Aohua Qian ◽  
George Hyatt ◽  
Andres Schanzer ◽  
Rohan Hazra ◽  
Abigail S. Hackam ◽  
...  
Keyword(s):  
Amino Acids ◽  
White Perch ◽  
Partial Agonist ◽  
Reversal Potential ◽  
Open Reading Frame ◽  
Retinal Neurons ◽  
Base Pairs ◽  
Reading Frame ◽  
A Value ◽  
Gabac Receptors

AbstractThere is increasing evidence that GABAC receptors are composed of GABA ρ subunits. In this study, we compared the properties of native GABAC receptors with those of receptors composed of a GABA ρ subunit. A homologue of the GABA ρ gene was cloned from a white perch (Roccus americana) retinal cDNA library. The clone (perch-s) has an open reading frame of 1422 nucleotide base pairs and encodes a predicted protein of 473 amino acids. It is highly homologous to GABA ρ subunits cloned from human and rat retinas. The receptors (perch-s receptor) expressed by this gene in Xenopus oocytes show properties similar to those of the GABAC receptors present on white perch retinal neurons. GABA induced a sustained response that had a reversal potential of –27.1 +minus; 3.6 mV. The EC50 for the response was 1.74 +− 1.25 μM, a value similar to that reported for GABAC receptors. Pharmacologically, the responses were bicuculline insensitive and not modulated by either diazepam or pentobarbital as is the case for GABAc receptors. There were, however, some distinct differences between native GABAc and perch-s receptors. I4AA acts as a partial agonist on perch-s receptors whereas it is strictly an antagonist on native GABAC receptors. Picrotoxin inhibition is noncompetitive on perch-s receptors, but both competitive and noncompetitive on GABAC receptors. We conclude that GABAC receptors are formed by GABA p subunits but that native GABAc receptors probably consist of a mixture of GABA ρ subunits.

scholarly journals Identification and Characterization of the Diverse Stress-Responsive R2R3-RMYB Transcription Factor from Hibiscus sabdariffa L.

2017 ◽  
Vol 2017 ◽  
pp. 1-12
Author(s):  
Bahaeldeen Babikar Mohamed ◽  
Beenish Aftab ◽  
Muhammad Bilal Sarwar ◽  
Bushra Rashid ◽  
Zarnab Ahmad ◽  
...  
Keyword(s):  
Amino Acids ◽  
Transcription Factor ◽  
In Silico Analysis ◽  
Healthy Plant ◽  
Hibiscus Sabdariffa ◽  
Reading Frame ◽  
Plant Expression Vector ◽  
Random Amplification ◽  
Cotton Cultivar

Various regulatory proteins play a fundamental role to manage the healthy plant growth under stress conditions. Differential display reverse transcriptase PCR and random amplification of cDNA ends (RACE) was used to explore the osmotic stress-responsive transcripts. We identified and characterized the salt stress-responsive R2R3 type RMYB transcription factor from Hibiscus sabdariffa which has an open reading frame of 690 bp, encoding 229 long chain amino acids. In silico analysis confirmed the conserved R2 and R3 domain as well as an NLS-1 localization site. The deduced amino acids of RMYB shared 83, 81, 80, 79, 72, 71, and 66% homology with Arabidopsis thaliana, Glycine max, Oryza sativa, Zea maize, Malus domestica, Populus tremula × Populus alba, and Medicago sativa specific MYB family, respectively. We observed the gene upregulation in stem, leaf, and root tissue in response to abiotic stress. Furthermore, RMYB gene was cloned into plant expression vector under CaMV35S promoter and transformed to Gossypium hirsutum: a local cotton cultivar. Overexpression of RMYB was observed in transgenic plants under abiotic stresses which further suggests its regulatory role in response to stressful conditions. The RMYB transcription factor-overexpressing in transgenic cotton plants may be used as potential agent for the development of stress tolerant crop cultivars.

scholarly journals Characterization of the rat transforming growth factor alpha gene and identification of promoter sequences.

1990 ◽  
Vol 10 (5) ◽  
pp. 2111-2121 ◽  
Author(s):  
A J Blasband ◽  
K T Rogers ◽  
X R Chen ◽  
J C Azizkhan ◽  
D C Lee
Keyword(s):  
Amino Acids ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Alpha ◽  
Base Pairs ◽  
S1 Nuclease ◽  
Reading Frame ◽  
Nuclear Extracts ◽  
Factor Alpha

We have determined the complete nucleotide sequence of rat transforming growth factor alpha (TGF alpha) mRNA and characterized the six exons that encode this transcript. These six exons span approximately 85 kilobases of genomic DNA, with exons 1 to 3 separated by particularly large introns. What had previously been thought to represent a species-specific difference in the size of the TGF alpha precursor (proTGF alpha) is now shown to be due to microheterogeneity in the splicing of exons 2 and 3. This results from a tandem duplication of the acceptor CAG and gives rise to two alternate forms (159 and 160 amino acids) of the integral membrane precursor. Exon 6, which encodes the 3' untranslated region of TGF alpha mRNA, also encodes, on the opposite strand, a small (approximately 200-nucleotide) transcript whose sequence predicts an open reading frame of 51 amino acids. Expression of this latter transcript does not appear to be coregulated with that of TGF alpha mRNA. Primer extension and S1 nuclease analyses of authentic TGF alpha transcripts revealed two major and multiple minor 5' ends which span more than 200 base pairs of DNA in a G + C-rich region that lacks canonical CCAAT or TATA sequences. The 5' ends of six independently derived cDNAs localized to five different sites in this same region. Restriction fragments that overlap these transcription start sites and extend approximately 300 base pairs in the 5' direction faithfully promote transcription in vitro with HeLa cell nuclear extracts. In addition, they direct the expression of the bacterial chloramphenicol acetyltransferase gene in transient-transfection assays.

scholarly journals Characterization of the rat transforming growth factor alpha gene and identification of promoter sequences

1990 ◽  
Vol 10 (5) ◽  
pp. 2111-2121
Author(s):  
A J Blasband ◽  
K T Rogers ◽  
X R Chen ◽  
J C Azizkhan ◽  
D C Lee
Keyword(s):  
Amino Acids ◽  
Growth Factor ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Alpha ◽  
Base Pairs ◽  
S1 Nuclease ◽  
Reading Frame ◽  
Nuclear Extracts ◽  
Factor Alpha

We have determined the complete nucleotide sequence of rat transforming growth factor alpha (TGF alpha) mRNA and characterized the six exons that encode this transcript. These six exons span approximately 85 kilobases of genomic DNA, with exons 1 to 3 separated by particularly large introns. What had previously been thought to represent a species-specific difference in the size of the TGF alpha precursor (proTGF alpha) is now shown to be due to microheterogeneity in the splicing of exons 2 and 3. This results from a tandem duplication of the acceptor CAG and gives rise to two alternate forms (159 and 160 amino acids) of the integral membrane precursor. Exon 6, which encodes the 3' untranslated region of TGF alpha mRNA, also encodes, on the opposite strand, a small (approximately 200-nucleotide) transcript whose sequence predicts an open reading frame of 51 amino acids. Expression of this latter transcript does not appear to be coregulated with that of TGF alpha mRNA. Primer extension and S1 nuclease analyses of authentic TGF alpha transcripts revealed two major and multiple minor 5' ends which span more than 200 base pairs of DNA in a G + C-rich region that lacks canonical CCAAT or TATA sequences. The 5' ends of six independently derived cDNAs localized to five different sites in this same region. Restriction fragments that overlap these transcription start sites and extend approximately 300 base pairs in the 5' direction faithfully promote transcription in vitro with HeLa cell nuclear extracts. In addition, they direct the expression of the bacterial chloramphenicol acetyltransferase gene in transient-transfection assays.

scholarly journals Molecular Cloning, Characterization, and Potential Roles of Cytosolic and Mitochondrial Aldehyde Dehydrogenases in Ethanol Metabolism in Saccharomyces cerevisiae

1998 ◽  
Vol 180 (4) ◽  
pp. 822-830 ◽  
Author(s):  
Xinping Wang ◽  
Craig J. Mann ◽  
Yinlin Bai ◽  
Li Ni ◽  
Henry Weiner
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Genomic Sequence ◽  
Divalent Cations ◽  
Open Reading Frame ◽  
Ethanol Metabolism ◽  
Reading Frame ◽  
Genes Encoding ◽  
Dna Fragment

ABSTRACT The full-length DNAs for two Saccharomyces cerevisiaealdehyde dehydrogenase (ALDH) genes were cloned and expressed inEscherichia coli. A 2,744-bp DNA fragment contained an open reading frame encoding cytosolic ALDH1, with 500 amino acids, which was located on chromosome XVI. A 2,661-bp DNA fragment contained an open reading frame encoding mitochondrial ALDH5, with 519 amino acids, of which the N-terminal 23 amino acids were identified as the putative leader sequence. The ALDH5 gene was located on chromosome V. The commercial ALDH (designated ALDH2) was partially sequenced and appears to be a mitochondrial enzyme encoded by a gene located on chromosome XV. The recombinant ALDH1 enzyme was found to be essentially NADP dependent, while the ALDH5 enzyme could utilize either NADP or NAD as a cofactor. The activity of ALDH1 was stimulated two- to fourfold by divalent cations but was unaffected by K+ ions. In contrast, the activity of ALDH5 increased in the presence of K+ ions: 15-fold with NADP and 40-fold with NAD, respectively. Activity staining of isoelectric focusing gels showed that cytosolic ALDH1 contributed 30 to 70% of the overall activity, depending on the cofactor used, while mitochondrial ALDH2 contributed the rest. Neither ALDH5 nor the other ALDH-like proteins identified from the genomic sequence contributed to the in vitro oxidation of acetaldehyde. To evaluate the physiological roles of these three ALDH isoenzymes, the genes encoding cytosolic ALDH1 and mitochondrial ALDH2 and ALDH5 were disrupted in the genome of strain TWY397 separately or simultaneously. The growth of single-disruption Δald1 and Δald2 strains on ethanol was marginally slower than that of the parent strain. The Δald1 Δald2 double-disruption strain failed to grow on glucose alone, but growth was restored by the addition of acetate, indicating that both ALDHs might catalyze the oxidation of acetaldehyde produced during fermentation. The double-disruption strain grew very slowly on ethanol. The role of mitochondrial ALDH5 in acetaldehyde metabolism has not been defined but appears to be unimportant.

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