scholarly journals A novel porcine gene-<i>MGLL</i>, differentially expressed in the backfat tissues from Meishan and Large White pigs

2010 ◽  
Vol 53 (5) ◽  
pp. 555-563
Author(s):  
Y. Dawei ◽  
B. Baoliang ◽  
L. Yonggang
Keyword(s):  
Tissue Expression ◽  
Complete Sequence ◽  
Differentially Expressed ◽  
Computer Assisted ◽  
Large White ◽  
Reading Frame ◽  
Tissue Expression Analysis ◽  
Red Jungle Fowl ◽  
Monoglyceride Lipase ◽  
Rapid Amplification

Abstract. One novel gene that was differentially expressed was identified through semi-quantitative RT-PCR and the cDNA complete sequence was then obtained using the rapid amplification of cDNA ends (RACE) method. Nucleotide sequence of the gene is not homologous to any of the known porcine genes. The sequence prediction analysis revealed that the open reading frame of this gene encodes a protein of 303 amino acids has high homology with the monoglyceride lipase (MGLL) of eight species-dog (91 %), human (89 %), cattle (88 %), platypus (83 %), mouse (82 %), rat (81 %), rhesus monkey (80 %), and red jungle fowl (70 %) – so that it can be defined as swine MGLL gene. This gene is structured in seven exons and six introns as revealed by computer-assisted analysis. The tissue expression analysis indicated that the swine MGLL gene is differentially expressed in detected tissues. Our experiment suggested that the swine MGLL gene might play an important roles in the superabundant fat deposition of Chinese pigs.

scholarly journals A novel porcine gene, USP7, differentially expressed in the musculus longissimus from Wujin and Large White pigs

2010 ◽  
Vol 55 (No. 1) ◽  
pp. 37-41
Author(s):  
Liu Yongganmg ◽  
Gao Shizheng
Keyword(s):  
Gene Expression ◽  
Differentially Expressed Gene ◽  
Differentially Expressed ◽  
Rt Pcr ◽  
Large White ◽  
Reading Frame ◽  
Sequence Prediction ◽  
Porcine Gene ◽  
Rapid Amplification ◽  
Display Technique

The mRNA differential display technique was performed to investigate differences in the gene expression in the <I>musculus longissimus</I> from Wujin and Large White pigs. A fragment of one differentially expressed gene was isolated and sequenced. A complete cDNA sequence was obtained using the rapid amplification of cDNA ends (RACE) method. The sequence prediction analysis revealed that the open reading frame of this gene encodes a protein of 1 103 amino acids, which is homologous with the ubiquitin specific peptidase 7 (<I>USP7</I>) of four species, rat (identity 98%), human (98%), mouse (98%) and chicken (95%), so it can be defined as the porcine <I>USP7</I> gene. The differences in the USP7 gene expression in muscles from Wujin and Large White pigs were confirmed using semi-quantitative RT-PCR. The gene expression analysis in eight tissues of a Wujin × Large White cross showed that <I>USP7</I> was expressed in all the tissues, except for fat.

scholarly journals Initial Characterization and Expression Pattern Analysis of Tobacco (Nicotiana Tabacum) 2-Hydroxyisoflavanone Dehydratasedase Gene

2021 ◽  
Vol 292 ◽  
pp. 03098
Author(s):  
Meiwei Zhao ◽  
Song Miao ◽  
Jun Guo ◽  
Yongyu Li ◽  
Zhengxiong Zhao
Keyword(s):  
Nicotiana Tabacum ◽  
Profile Analysis ◽  
Tissue Expression ◽  
Reading Frame ◽  
Lycopersicon Pennellii ◽  
Nicotiana Tomentosiformis ◽  
Expression Profile Analysis ◽  
Tissue Expression Profile ◽  
Rapid Amplification ◽  
Single Exon Gene

The complete mRNA sequence of one tobacco (nicotiana tabacum) gene—2-hydroxyisoflavanone dehydratasedase, was amplified using the rapid amplification of cDNA ends methods based on one tobacco EST. The full-length tobacco 2-hydroxyisoflavanone dehydratasedase gene mRNA was 1,278bp containing a 966 bp open reading frame, which encodes a protein of 321 amino acids. Sequence analysis revealed that the 2-hydroxyisoflavanone dehydratasedase of tobacco shares high homology with the 2-hydroxyisoflavanone dehydratasedase of nicotiana tomentosiformis(99%), capsicum annuum(78%), potato(75%), lycopersicon pennellii(73%) and lycopersicon esculentum(72%). BLAST analysis within the tobacco high throughout genomic sequences database revealed that this gene has no intron and is a single exon gene. Results also showed that tobacco 2-hydroxyisoflavanone dehydratasedase gene has a closer genetic relationship with the 2-hydroxyisoflavanone dehydratasedase gene of nicotiana tomentosiformis. Tissue expression profile analysis revealed that the tobacco 2-hydroxyisoflavanone dehydratasedase gene was highly expressed in leaf and flower, but moderately expressed in root and stem. Our experiment established the foundation for further research on this tobacco gene.

scholarly journals Molecular characterization and expression analysis of the NLR family CARD containing five transcripts in the pig

2016 ◽  
Vol 19 (4) ◽  
pp. 753-761 ◽  
Author(s):  
Q.Y. Yang ◽  
T. Chen ◽  
Y.B. Chen ◽  
D.L. Lan
Keyword(s):  
Lymph Node ◽  
Expression Analysis ◽  
Cdna Sequence ◽  
Evolutionary Relationship ◽  
Tissue Expression ◽  
Vital Role ◽  
Reading Frame ◽  
Tissue Expression Analysis ◽  
Organ Systems ◽  
Comparative Immunity

Abstract The NOD-like receptor (NLR) family caspase recruitment domain-containing 5 (NLRC5) is one of the newly discovered and largest NLR family members. The NLRC5 has recently received extensive attention because of its important role in regulating innate and adaptive immune responses. The NLRC5 in many vertebrates, such as humans, mice, cattle, and horses, has already been proven and studied. However, the NLRC5 gene characteristics of pigs remain unclear. Thus, we completely cloned the NLRC5 cDNA sequence of the pig using the rapid amplification of cDNA ends(RACE) technology. A characteristic and tissue expression analysis was also conducted on the pig sequence. The sequence analysis showed that the complete cDNA sequence of the NLRC5 of the pig is 6638 bp, and the open reading frame is 5538 bp which encoded 1846 amino acids. The protein prediction analysis indicates that the overall performance of the NLRC5 protein of the pig is hydrophilic and possesses a typical nucleotide binding and oligomerization domain(NBD) and 20 leucine-rich repeats(LRRs). The homology analysis result indicates that the NLRC5 transcript in pigs is highly homologous to cattle, sheep, macaques, and humans, and accounts for around 80%. The genetic evolutionary tree analysis shows that the NLRC5 transcript in pigs has the closest evolutionary relationship with cattle and sheep. Further tissue expression analysis shows that immune organ systems (e.g., lymph node and spleen) and mucosa organs (e.g., intestinal lymph node, stomach, and lungs) possess high expressions with NLRC5 mRNA. The result of this study indicates that the NLRC5 transcript in pigs is relatively conservative among mammals and may play a vital role in immune reaction, which provides a basis for further studies on the NLRC5 function in the pig immune system and the role in comparative immunity.

scholarly journals Gene Cloning and Tissue Expression Analysis of a PR-5 Thaumatin-Like Protein in Phellinus weirii-Infected Douglas-Fir

2004 ◽  
Vol 94 (11) ◽  
pp. 1235-1243 ◽  
Author(s):  
Arezoo Zamani ◽  
Rona N. Sturrock ◽  
Abul K. M. Ekramoddoullah ◽  
Jun Jun Liu ◽  
Xueshu Yu
Keyword(s):  
Amino Acid ◽  
Immunoblot Analysis ◽  
Tissue Expression ◽  
Douglas Fir ◽  
Coding Region ◽  
General Role ◽  
Peptide Cleavage ◽  
Reading Frame ◽  
Tissue Expression Analysis ◽  
Phellinus Weirii

In western North America, Douglas-fir (Pseudotsuga menziesii) is the most economically important conifer species susceptible to laminated root rot caused by Phellinus weirii. While attempting to internally sequence an endochitinase found to be up-regulated in P. weirii-infected Douglas-fir roots, we obtained overlapping peptide fragments showing 28% similarity with a PR-5 thaumatin-like protein (TLP) designated PmTLP (Pm for Pseudotsuga menziesi). A rabbit polyclonal antibody was reared against a synthetic peptide composed of a 29-amino-acid-long, conserved, internal sequence of PmTLP and purified by immunoaffinity. Western immunoblot analysis of infected roots of 24-year-old coastalfir showed significantly higher amounts of PmTLP (P < 0.01) closest to the point of P. weirii inoculation and infection than in uninfected regions of the same root. The antibody was also used to screen for PmTLP in roots of 25-year-old interior Douglas-firs naturally infected with a related pathogen, Armillaria ostoyae, and results showed significantly higher levels of PmTLP in bark tissues adjacent to infection (P < 0.05) than in uninfected tissue. Using polymerase chain reaction (PCR)-based cloning, the cDNA of PmTLP was shown to have a 702-bp open reading frame with a signal peptide cleavage site at 155 bp corresponding to a 29-amino-acid-long residue prior to the start of the N-terminal. Based on the deduced amino acid sequence, the molecular mass of the putative PmTLP was calculated to be 21.0 kDa with an isoelectric point of 3.71. Alignment analysis of PmTLP cDNA with a representative genomic DNA PCR sequence showed presence of one intron of variable size, within the coding region. The induction of PmTLP at the site of root infection and its presence in needle tissue suggests a general role for this protein in adaptation to stress and may be part of an integrated defense response initiated by the host to impede further pathogen spread.

scholarly journals Initial Characterization and Expression Pattern Analysis of Tobacco (Nicotiana Tabacum) HMGS Gene

2021 ◽  
Vol 292 ◽  
pp. 03094
Author(s):  
Meiwei Zhao ◽  
Tao Zhang ◽  
Lei Yang ◽  
Hongtao Feng ◽  
Zhengxiong Zhao
Keyword(s):  
Nicotiana Tabacum ◽  
Withania Somnifera ◽  
Profile Analysis ◽  
Nicotiana Sylvestris ◽  
Tissue Expression ◽  
Nicotiana Attenuata ◽  
Reading Frame ◽  
Expression Profile Analysis ◽  
Tissue Expression Profile ◽  
Rapid Amplification

3-hydroxy-3-methylglutaryl coenzyme A synthase (HMGS) is a member of condensing enzymes that catalyze a Claisen-like condensation reaction.The tobacco (nicotiana tabacum) HMGS gene was firstly characterized using the rapid amplification of cDNA ends methods based on one tobacco EST. The full-length tobacco HMGS gene mRNA was 1,773bp containing a 1389 bp open reading frame, which encodes a protein of 462 amino acids. Sequence analysis revealed that the HMGS of tobacco shares high homology with the HMGS of nicotiana tomentosiformis (96%), nicotiana attenuata (95%), Nicotiana sylvestris (95%), nicotiana benthamiana(94%), solanum lycopersicum(94%), solanum tuberosum(93%) and withania somnifera(93%). Results also showed that tobacco HMGS gene has a closer genetic relationship with the HMGS gene of withania somnifera. Tissue expression profile analysis revealed that the tobacco HMGS gene was highly expressed in flower, but moderately expressed in leaf and stem, and weakly expressed in root. Our experiment established the foundation for further research on this tobacco gene.

scholarly journals Initial Characterization and Expression Pattern Analysis of Tobacco (Nicotiana Tabacum) GMP Synthase Gene

2021 ◽  
Vol 292 ◽  
pp. 03070
Author(s):  
Meiwei Zhao ◽  
Lei Yang ◽  
Jiacan Wu ◽  
Haijuan Wang ◽  
Zhengxiong Zhao
Keyword(s):  
Nicotiana Tabacum ◽  
Profile Analysis ◽  
Tissue Expression ◽  
Guanosine Monophosphate ◽  
Nicotiana Attenuata ◽  
Reading Frame ◽  
Lycopersicon Pennellii ◽  
Expression Profile Analysis ◽  
Tissue Expression Profile ◽  
Rapid Amplification

The complete mRNA sequence of one tobacco (nicotiana tabacum) gene—guanosine monophosphate (GMP)synthase, was amplified using the rapid amplification of cDNA ends methods. The full-length tobacco GMP synthase gene mRNA was 2,127bp containing a 1,617 bp open reading frame, which encodes a protein of 538 amino acids. Sequence analysis revealed that the GMP synthase of tobacco shares high homology with the GMP synthase of wood tobacco(99%), nicotiana attenuata(99%), nicotiana tomentosiformis(99%), potato(92%), Lycopersicon pennellii(92%), lycopersicon esculentum(92%), capsicum annuum(91%), capsicum chinense(91%) and capsicum baccatum(90%). BLAST analysis within the tobacco high throughout genomic sequences database revealed that this gene has 5 introns and 6 exons. Results also showed that tobacco GMP synthase gene has a closer genetic relationship with the GMP synthase gene of wood tobacco. Tissue expression profile analysis revealed that the tobacco GMP synthase gene was highly expressed in leaf, but moderately expressed in root, flower and stem. Our experiment established the foundation for further research on this tobacco gene.

Molecular Cloning of a HMG-CoA Reductase Gene from Eucommia ulmoides Oliver

2006 ◽  
Vol 26 (2) ◽  
pp. 171-181 ◽  
Author(s):  
Jihong Jiang ◽  
Guoyin Kai ◽  
Xiaoying Cao ◽  
Fengmei Chen ◽  
Dongning He ◽  
...  
Keyword(s):  
Bioinformatic Analysis ◽  
Tissue Expression ◽  
Full Length ◽  
Eucommia Ulmoides ◽  
Phylogenetic Tree Analysis ◽  
Reading Frame ◽  
Full Length Cdna ◽  
Calculated Molecular Weight ◽  
Rapid Amplification ◽  
Coa Reductase

The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the conversion of HMG-CoA to mevalonate, which is the first committed step in the pathway for isoprenoid biosynthesis in plants. A full-length cDNA encoding HMGR (designated as EuHMGR, GenBank Accession No. AY796343) was isolated from Eucommia ulmoides by rapid amplification of cDNA ends (RACE). The full-length cDNA of EuHMGR comprises 2281 bp with a 1770-bp open reading frame (ORF) encoding a 590-amino-acid polypeptide with two trans-membrane domains revealed by bioinformatic analysis. Molecular modeling showed that EuHMGR is a new HMGR with a spatial structure similar to other plant HMGRs. The deduced protein has an isoelectric point (pI) of 6.89 and a calculated molecular weight of about 63 kDa. Sequence comparison analysis showed that EuHMGR had highest homology to HMGR from Hevea brasiliensis. As expected, phylogenetic tree analysis indicated that EuHMGR belongs to plant HMGR group. Tissue expression pattern analysis showed that EuHMGR is strongly expressed in the leaves and stems whereas it is only poorly expressed in the roots, which implies that EuHMGR may be a constitutively expressing gene. Functional complementation of EuHMGR in HMGR-deficient mutant yeast JRY2394 demonstrated that EuHMGR mediates the mevalonate biosynthesis in yeast.

scholarly journals Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein.

1989 ◽  
Vol 9 (6) ◽  
pp. 2615-2626 ◽  
Author(s):  
E Hickey ◽  
S E Brandon ◽  
G Smale ◽  
D Lloyd ◽  
L A Weber
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Normal Growth ◽  
Gene Families ◽  
Growth Conditions ◽  
Complete Sequence ◽  
Start Codon ◽  
Hybridization Probe ◽  
Reading Frame ◽  
Alpha Gene

Vertebrate cells synthesize two forms of the 82- to 90-kilodalton heat shock protein that are encoded by distinct gene families. In HeLa cells, both proteins (hsp89 alpha and hsp89 beta) are abundant under normal growth conditions and are synthesized at increased rates in response to heat stress. Only the larger form, hsp89 alpha, is induced by the adenovirus E1A gene product (M. C. Simon, K. Kitchener, H. T. Kao, E. Hickey, L. Weber, R. Voellmy, N. Heintz, and J. R. Nevins, Mol. Cell. Biol. 7:2884-2890, 1987). We have isolated a human hsp89 alpha gene that shows complete sequence identity with heat- and E1A-inducible cDNA used as a hybridization probe. The 5'-flanking region contained overlapping and inverted consensus heat shock control elements that can confer heat-inducible expression on a beta-globin reporter gene. The gene contained 10 intervening sequences. The first intron was located adjacent to the translation start codon, an arrangement also found in the Drosophila hsp82 gene. The spliced mRNA sequence contained a single open reading frame encoding an 84,564-dalton polypeptide showing high homology with the hsp82 to hsp90 proteins of other organisms. The deduced hsp89 alpha protein sequence differed from the human hsp89 beta sequence reported elsewhere (N. F. Rebbe, J. Ware, R. M. Bertina, P. Modrich, and D. W. Stafford (Gene 53:235-245, 1987) in at least 99 out of the 732 amino acids. Transcription of the hsp89 alpha gene was induced by serum during normal cell growth, but expression did not appear to be restricted to a particular stage of the cell cycle. hsp89 alpha mRNA was considerably more stable than the mRNA encoding hsp70, which can account for the higher constitutive rate of hsp89 synthesis in unstressed cells.

An electrogenic Na+- HCO 3 − cotransporter (NBC) with a novel COOH-terminus, cloned from rat brain

2000 ◽  
Vol 278 (6) ◽  
pp. C1200-C1211 ◽  
Author(s):  
Mark O. Bevensee ◽  
Bernhard M. Schmitt ◽  
Inyeong Choi ◽  
Michael F. Romero ◽  
Walter F. Boron
Keyword(s):  
Rat Brain ◽  
Cortical Neurons ◽  
Polyclonal Antibodies ◽  
Amino Acid Level ◽  
Cdna Libraries ◽  
Human Pancreas ◽  
Opposite Pattern ◽  
Reading Frame ◽  
Expression Studies ◽  
Rapid Amplification

We screened rat brain cDNA libraries and used 5′ rapid amplification of cDNA ends to clone two electrogenic Na+-[Formula: see text] cotransporter (NBC) isoforms from rat brain (rb1NBC and rb2NBC). At the amino acid level, one clone (rb1NBC) is 96% identical to human pancreas NBC. The other clone (rb2NBC) is identical to rb1NBC except for 61 unique COOH-terminal amino acids, the result of a 97-bp deletion near the 3′ end of the open-reading frame. Using RT-PCR, we confirmed that mRNA from rat brain contains this 97-bp deletion. Furthermore, we generated rabbit polyclonal antibodies that distinguish between the unique COOH-termini of rb1NBC (αrb1NBC) and rb2NBC (αrb2NBC). αrb1NBC labels an ∼130-kDa protein predominantly from kidney, and αrb2NBC labels an ∼130-kDa protein predominantly from brain. αrb2NBC labels a protein that is more highly expressed in cortical neurons than astrocytes cultured from rat brain; αrb1NBC exhibits the opposite pattern. In expression studies, applying 1.5% CO2/10 mM [Formula: see text] to Xenopus oocytes injected with rb2NBC cRNA causes 1) pHi to recover from the initial CO2-induced acidification and 2) the cell to hyperpolarize. Subsequently, removing external Na+ reverses the pHi increase and elicits a rapid depolarization. In the presence of 450 μM DIDS, removing external Na+ has no effect on pHi and elicits a small hyperpolarization. The rate of the pHidecrease elicited by removing Na+ is insensitive to removing external Cl−. Thus rb2NBC is a DIDS-sensitive, electrogenic NBC that is predominantly expressed in brain of at least rat.

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