scholarly journals Insertion of an endogenous Jaagsiekte sheep retrovirus element into the BCO2 - gene abolishes its function and leads to yellow discoloration of adipose tissue in Norwegian Spælsau (Ovis aries)

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Matthew Kent ◽  
Michel Moser ◽  
Inger Anne Boman ◽  
Kristine Lindtveit ◽  
Mariann Árnyasi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Adipose Tissue ◽  
Amino Acid ◽  
Nonsense Mutation ◽  
Ovis Aries ◽  
Splice Acceptor Site ◽  
Recessive Trait ◽  
Hybrid Protein ◽  
Jaagsiekte Sheep Retrovirus ◽  
Enzymatic Function

Abstract Background The accumulation of carotenoids in adipose tissue leading to yellow fat is, in sheep, a heritable recessive trait that can be attributed to a nonsense mutation in the beta-carotene oxygenase 2 (BCO2) gene. However, not all sheep breeds suffering from yellow fat have this nonsense mutation, meaning that other functional mechanisms must exist. We investigated one such breed, the Norwegian spælsau. Results In spælsau we detected an aberration in BCO2 mRNA. Nanopore sequencing of genomic DNA revealed the insertion of a 7.9 kb endogenous Jaagsiekte Sheep Retrovirus (enJSRV) sequence in the first intron of the BCO2 gene. Close examination of its cDNA revealed that the BCO2 genes first exon was spliced together with enJSRV-sequence immediately downstream of a potential -AG splice acceptor site at enJSRV position 415. The hybrid protein product consists of 29 amino acids coded by the BCO2 exon 1, one amino acid coded by the junction sequence, followed by 28 amino acids arbitrary coded for by the enJSRV-sequence, before a translation stop codon is reached. Conclusions Considering that the functional BCO2 protein consists of 575 amino acids, it is unlikely that the 58 amino acid BCO2/enJSRV hybrid protein can display any enzymatic function. The existence of this novel BCO2 allele represents an alternative functional mechanism accounting for BCO2 inactivation and is a perfect example of the potential benefits for searching for structural variants using long-read sequencing data.

scholarly journals Insertion of an endogenous Jaagsiekte Sheep Retrovirus element into the BCO2 - gene abolishes its function and leads to yellow discoloration of adipose tissue in Norwegian Spælsau (Ovis aries)

2020 ◽  
Author(s):  
Matthew Kent ◽  
Michel Moser ◽  
Inger Anne Boman ◽  
Kristine Lindtveit ◽  
Mariann Árnyasi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Adipose Tissue ◽  
Nonsense Mutation ◽  
Ovis Aries ◽  
Splice Acceptor Site ◽  
Acceptor Site ◽  
Recessive Trait ◽  
Hybrid Protein ◽  
Jaagsiekte Sheep Retrovirus ◽  
Enzymatic Function

AbstractBackgroundThe accumulation of carotenoids in adipose tissue leading to yellow fat is, in sheep, a heritable recessive trait that can be attributed to a nonsense mutation in the beta-carotene oxygenase 2 (BCO2) gene. However, not all sheep breeds suffering from yellow fat have this nonsense mutation, meaning that other functional mechanisms must exist. We investigated one such breed, the Norwegian spælsau.ResultsIn spælsau we detected an aberration in BCO2 mRNA. Nanopore sequencing of genomic DNA revealed the insertion of a 7.9 kb endogenous Jaagsiekte Sheep Retrovirus (enJSRV) sequence in the first intron of the BCO2 gene. Close examination of its cDNA revealed that the BCO2 genes first exon was spliced together with enJSRV-sequence immediately downstream of a potential - AG splice acceptor site at enJSRV position 415. The hybrid protein product consists of 29 amino acids coded by the BCO2 exon 1, followed by 29 amino acids arbitrary coded for by the enJSRV-sequence, before a translation stop codon is reached.ConclusionsConsidering that the functional BCO2 protein consists of 575 amino acids, it is unlikely that the 58 amino acid BCO2/enJSRV hybrid protein can display any enzymatic function. The existence of this novel BCO2 allele represents an alternative functional mechanism accounting for BCO2 inactivation and is a perfect example of the potential benefits for searching for structural variants using long-read sequencing data.

scholarly journals Effects of dietary n-6:n-3 PUFA ratio on fatty acid composition, free amino acid profile and gene expression of transporters in finishing pigs

2015 ◽  
Vol 113 (5) ◽  
pp. 739-748 ◽  
Author(s):  
Fengna Li ◽  
Yehui Duan ◽  
Yinghui Li ◽  
Yulong Tang ◽  
Meimei Geng ◽  
...  
Keyword(s):  
Amino Acids ◽  
Adipose Tissue ◽  
Fatty Acid ◽  
Amino Acid ◽  
Subcutaneous Adipose Tissue ◽  
Longissimus Dorsi ◽  
Finishing Pigs ◽  
Mrna Expression Level ◽  
Pufa Ratio ◽  
Subcutaneous Adipose

Revealing the expression patterns of fatty acid and amino acid transporters as affected by dietary n-6:n-3 PUFA ratio would be useful for further clarifying the importance of the balance between n-6 and n-3 PUFA. A total of ninety-six finishing pigs were fed one of four diets with the ratio of 1:1, 2·5:1, 5:1 and 10:1. Pigs fed the dietary n-6:n-3 PUFA ratio of 5:1 had the highest (P< 0·05) daily weight gain, and those fed the dietary n-6:n-3 PUFA ratio of 1:1 had the largest loin muscle area (P< 0·01). The concentration of n-3 PUFA was raised as the ratio declined (P< 0·05) in the longissimus dorsi and subcutaneous adipose tissue. The contents of tryptophan, tasty amino acids and branched-chain amino acids in the longissimus dorsi were enhanced in pigs fed the dietary n-6:n-3 PUFA ratios of 1:1–5:1. The mRNA expression level of the fatty acid transporter fatty acid transport protein-1 (FATP-1) was declined (P< 0·05) in the longissimus dorsi of pigs fed the dietary n-6:n-3 PUFA ratios of 1:1–5:1, and increased (P< 0·05) in the subcutaneous adipose tissue of pigs fed the dietary n-6:n-3 PUFA ratios of 5:1 and 10:1. The expression profile of FATP-4 was similar to those of FATP-1 in the adipose tissue. The mRNA expression level of the amino acid transceptors LAT1 and SNAT2 was up-regulated (P< 0·05) in the longissimus dorsi of pigs fed the dietary n-6:n-3 PUFA ratios of 1:1 and 2·5:1. In conclusion, maintaining the dietary n-6:n-3 PUFA ratios of 1:1–5:1 would facilitate the absorption and utilisation of fatty acids and free amino acids, and result in improved muscle and adipose composition.

scholarly journals Non-enzymatic assembly of active chimeric ribozymes from aminoacylated RNA oligonucleotides

2021 ◽  
Author(s):  
Aleksandar Radakovic ◽  
Saurja Dasgupta ◽  
Tom H Wright ◽  
Harry R.M. Aitken ◽  
Jack W Szostak
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Ribosomal Protein ◽  
Rna World ◽  
Directed Assembly ◽  
Enzymatic Function ◽  
Hammerhead Rna ◽  
Rna Backbone ◽  
Ribosomal Protein Synthesis

Aminoacylated tRNAs, which harbor a covalent linkage between amino acids and RNA, are a universally conserved feature of life. Because they are essential substrates for ribosomal translation, aminoacylated oligonucleotides must have been present in the RNA World prior to the evolution of the ribosome. One possibility we are exploring is that the aminoacyl ester linkage served another function before being recruited for ribosomal protein synthesis. The nonenzymatic assembly of ribozymes from short RNA oligomers under realistic conditions remains a key challenge in demonstrating a plausible pathway from prebiotic chemistry to the RNA World. Here, we show that aminoacylated RNAs can undergo template-directed assembly into chimeric amino acid-RNA polymers that are active ribozymes. We demonstrate that such chimeric polymers can retain the enzymatic function of their all-RNA counterparts by generating chimeric hammerhead, RNA ligase, and aminoacyl transferase ribozymes. Amino acids with diverse side chains form linkages that are well tolerated within the RNA backbone, potentially bringing novel functionalities to ribozyme catalysis. Our work suggests that aminoacylation chemistry may have played a role in primordial ribozyme assembly. Increasing the efficiency of this process provides an evolutionary rationale for the emergence of sequence and amino acid specific aminoacyl-RNA synthetase ribozymes, which could then have generated the substrates for ribosomal protein synthesis.

Molecular Cloning, Primary Sequence Characterization and Phylogentic Analysis of Cathepsin B cysteine from Sheep (Ovis aries) Ovarian

2020 ◽  
Author(s):  
Aiju Liu ◽  
Menghe Liu ◽  
Xin Qi ◽  
Xiaofei Ma ◽  
Heling Huang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Sites ◽  
Ovis Aries ◽  
Sequence Motif ◽  
Coding Sequence ◽  
Sequence Characterization ◽  
Conserved Sequence ◽  
Random Coils

Background: CathepsinB (CTSB) is a lysosomal cysteine protease which has been implicated in a variety of physiological and pathological processes. However, the sequence and structure characteristics of sheep CTSB gene are still unclear, which severely restricts the further study about genetic variation, molecular evolution.Methods: Therefore the coding sequence (CDS) of sheep CTSB gene from ovary was cloned by reverse transcription PCR (RT-PCR) amplification and regular sequencing technology. The characteristics of nucleotide and amino acid sequence of CTSB gene were analyzed through bioinformatics and the phylogenetic tree was constructed employing the Bayesian inference based on amino acid sequence of different species in this study.Result: A complete coding sequence of 1008 bp of CTSB was obtained from ovary, which encoded 335 amino acids. Functional prediction of CTSB protein suggested that containing five conserved sequence motif sites in which the site of amino acids between 158 and 205 was the most conserved region. Secondary structure analysis showed that á-helices were the major structure at the N-terminus, while random coils were the major structure at the C-terminus. Additionally, the motif II in the random coils, in which two active sites of His278 and Asn298 were located therein, was more conserved. The high similarity of CTSB amino acids alignment between sheep and other species recommended that CTSB was highly conservative in the evolutionary process.

Tryptophan-Requiring Mutants of the Plant Arabidopsis thaliana

Science ◽  
1988 ◽  
Vol 240 (4850) ◽  
pp. 305-310 ◽  
Author(s):  
ROBERT L. LAST ◽  
GERALD R. FINK
Keyword(s):  
Amino Acids ◽  
Arabidopsis Thaliana ◽  
Amino Acid ◽  
Second Step ◽  
Recessive Trait ◽  
Whole Plant ◽  
Tryptophan Pathway ◽  
Morphological Defects ◽  
Plant Level ◽  
Plant Arabidopsis Thaliana

Although amino acid auxotrophs are among the most frequently isolated mutations in microorganisms, no mutants that require amino acids have been isolated at the whole plant level. Tryptophan-requiring mutants of the cruciferous plant Arabidopsis thaliana have now been isolated by selecting for resistance to 5-methylanthranilic acid. The tryptophan requirement of one mutant, trpl-1, results from a defect in the second step of the tryptophan pathway catalyzed by anthranilate phosphoribosyl transferase. Mutant trpl-1 plants are highly fluorescent and aromatic because they accumulate anthranilic acid and anthranilate β-glucoside. Plants homozygous for the trpl-1 mutation exhibit a syndrome of morphological defects suggestive of a defect in the biosynthesis, metabolism, or localization of a tryptophan derivative such as auxin. All of these morphological phenotypes cosegregate with the tryptophan requirement as a simple Mendelian recessive trait.

Immunological detection of cDNA clones encoding the uncoupling protein of brown adipose tissue: Evidence for an antigenic determinant within the C-terminal eleven amino acids

1986 ◽  
Vol 6 (1) ◽  
pp. 87-94 ◽  
Author(s):  
Robert G. Ridley ◽  
Hasmukh V. Patel ◽  
Craig L. J. Parfett ◽  
Kimberly A. Olynyk ◽  
Susanna Reichling ◽  
...  
Keyword(s):  
Amino Acids ◽  
Adipose Tissue ◽  
Amino Acid ◽  
Brown Adipose Tissue ◽  
Antigenic Determinant ◽  
Uncoupling Protein ◽  
Cdna Clones ◽  
Amino Acid Homology ◽  
Brown Adipose ◽  
Uncoupling Protein Mrna

Poly(A)+ RNA was isolated from brown adipose tissue of cold acclimated rats and a fraction enriched for uncoupling protein mRNA was used to generate a cDNA library in pBR 322, Immunological screening of 1,500 colonies with an affinity-purified antiserum against the uncoupling protein yielded five positive clones, pUCPratl–5. Clone pUCPrat2 encoded the C-terminal 54 amino acids of rat uncoupling protein and exhibited 90% amino acid homology with the hamster protein. Clones pUCPrat3–5 encoded only the C-terminal 11 amino acids suggesting that an antigenic determinant lies within this sequence.

scholarly journals Amino acid and glucose uptake by rat brown adipose tissue. Effect of cold-exposure and acclimation

1988 ◽  
Vol 252 (3) ◽  
pp. 843-849 ◽  
Author(s):  
F J López-Soriano ◽  
J A Fernández-López ◽  
T Mampel ◽  
F Villarroya ◽  
R Iglesias ◽  
...  
Keyword(s):  
Amino Acids ◽  
Adipose Tissue ◽  
Amino Acid ◽  
Brown Adipose Tissue ◽  
Glucose Uptake ◽  
Cold Acclimation ◽  
Cold Exposure ◽  
Acid Oxidation ◽  
Interscapular Brown Adipose Tissue ◽  
Brown Adipose

The net uptake/release of glucose, lactate and amino acids from the bloodstream by the interscapular brown adipose tissue of control, cold-exposed and cold-acclimated rats was estimated by measurement of arteriovenous differences in their concentrations. In the control animals amino acids contributed little to the overall energetic needs of the tissue; glucose uptake was more than compensated by lactate efflux. Cold-exposure resulted in an enhancement of amino acid utilization and of glucose uptake, with high lactate efflux. There was a net glycine and proline efflux that partly compensated the positive nitrogen balance of the tissue; amino acids accounted for about one-third of the energy supplied by glucose to the tissue. Cold-acclimation resulted in a very high increase in glucose uptake, with a parallel decrease in lactate efflux and amino acid consumption. Branched-chain amino acids, however, were more actively utilized. This was related with a much higher alanine efflux, in addition to that of glycine and proline. It is suggested that most of the glucose used during cold-exposure is returned to the bloodstream as lactate under conditions of active lipid utilization, amino acids contributing their skeletons largely in anaplerotic pathways. On the other hand, cold-acclimation resulted in an important enhancement of glucose utilization, with lowered amino acid oxidation. Amino acids are thus used as metabolic substrates by the brown adipose tissue of rats under conditions of relatively scarce substrate availability, but mainly as anaplerotic substrates, in parallel to glucose. Cold-acclimation results in a shift of the main substrates used in thermogenesis from lipid to glucose, with a much lower need for amino acids.

scholarly journals Translation of Two Nested Genes in Bacteriophage P4 Controls Immunity-Specific Transcription Termination

1999 ◽  
Vol 181 (17) ◽  
pp. 5225-5233 ◽  
Author(s):  
Francesca Forti ◽  
Simona Polo ◽  
Kirk B. Lane ◽  
Erich W. Six ◽  
Gianpiero Sironi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nonsense Mutation ◽  
Transcription Termination ◽  
Open Reading Frame ◽  
Terminal Part ◽  
Reading Frame ◽  
Bacteriophage P4 ◽  
Nested Genes ◽  
Nonsense Codons

ABSTRACT In phage P4, transcription of the left operon may occur from both the constitutive PLE promoter and the regulated PLL promoter, about 400 nucleotides upstream of PLE. A strong Rho-dependent termination site,timm , is located downstream of both promoters. When P4 immunity is expressed, transcription starting at PLE is efficiently terminated attimm , whereas transcription from PLL is immunity insensitive and reads throughtimm . We report the identification of two nested genes, kil and eta, located in the P4 left operon. The P4 kil gene, which encodes a 65-amino-acid polypeptide, is the first translated gene downstream of the PLE promoter, and its expression is controlled by P4 immunity. Overexpression of kil causes cell killing. This gene is the terminal part of a longer open reading frame,eta, which begins upstream of PLE. Theeta gene is expressed when transcription starts from the PLL promoter. Three likely start codons predict a size between 197 and 199 amino acids for the Eta gene product. Bothkil and eta overlap thetimm site. By cloning kil upstream of a tRNA reporter gene, we demonstrated that translation of thekil region prevents premature transcription termination attimm . This suggests that P4 immunity might negatively control kil translation, thus enabling transcription termination at timm . Transcription starting from PLL proceeds throughtimm . Mutations that create nonsense codons ineta caused premature termination of transcription starting from PLL. Suppression of the nonsense mutation restored transcription readthrough at timm . Thus, termination of transcription from PLL is prevented by translation of eta.

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