Phage P22 tail protein: gene and amino acid sequence

Biochemistry ◽  
1982 ◽  
Vol 21 (23) ◽  
pp. 5811-5815 ◽  
Author(s):  
Robert T. Sauer ◽  
William Krovatin ◽  
Anthony R. Poteete ◽  
Peter B. Berget
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Gene ◽  
Phage P22 ◽  
Tail Protein

Glycine cleavage enzyme complex: Rabbit H-protein cDNA sequence analysis and comparison to human, cow, and chicken

2000 ◽  
Vol 78 (6) ◽  
pp. 725-730 ◽  
Author(s):  
Francis Choy ◽  
Lisa Sharp ◽  
Derek A Applegarth
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Matrix Protein ◽  
Protein Gene ◽  
Mitochondrial Targeting ◽  
Reading Frame ◽  
Cleavage Enzyme ◽  
Glycine Cleavage ◽  
H Protein ◽  
Sequence Similarities

The H-protein is one of the four essential components (H-, L-, P-, and T-proteins) of the mammalian glycine cleavage enzyme complex, the major degradative pathway of glycine. We have isolated the full-length cDNA of the H-protein gene from the rabbit (Oryctolagus caniculus) by reverse transcription of liver poly-A mRNA and determined its nucleotide sequence (GenBank Acc. No. BankIt 318281 AF 231451). Similar to that in human, the rabbit H-protein gene possesses a 519-bp open reading frame that translates a 173-amino-acid (aa) protein. This reading frame is comprised of a 48-aa mitochondrial targeting sequence and a 125-aa residue that constitutes the mature mitochondrial matrix protein. In the mature protein region, there is a 95.5% nucleotide and 98.4% amino-acid sequence similarity to human. This conservation was also noted in the mature protein of the cow (Bos taurus) and chicken (Gallus domesticus), where there are a 94.1% and 85.3% nucleotide similarities, and 95.2% and 85.6% amino-acid sequence similarities, respectively. However, the targeting region is not as well conserved. Comparison of the rabbit targeting sequence to that in human, cow, and chicken reveals 84.0%, 79.2%, and 72.9% nucleotide, and 72.9%, 75.0%, and 54.2% amino-acid sequence similarities, respectively. These findings suggest that within the H-protein gene, the regions encoding the mitochondrial targeting and matrix protein may have evolved differently. Gene diversification in the former may reflect the species specificity in targeting proteins destined for the mitochondria, whereas homology in the latter suggests a very similar structure-function of the mature H-protein among these species. This homology in structure-function likely accounts for the observation that non-human H-protein can replace the human protein in the activity assay of the glycine cleavage enzyme system. This includes the biochemical diagnosis of non-ketotic hyperglycinemia (NKH) resulting from defects other than the H-protein, e.g., mutation(s) in the P-protein.Key words: glycine cleavage enzyme, H-protein, sequence comparison, non-ketotic hyperglycinemia.

scholarly journals Nucleotide sequence and deduced amino acid sequence of a new Lepidoptera-specific crystal protein gene fromBacillus thuringiensis

1990 ◽  
Vol 18 (18) ◽  
pp. 5545-5545 ◽  
Author(s):  
Herman Höfte ◽  
Piet Soetaert ◽  
Stefan Jansens ◽  
Marnix Peferoen
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Protein Gene ◽  
Crystal Protein

scholarly journals Biological, Pathological, and Molecular Characteristics of a New Potyvirus, Dendrobium Chlorotic Mosaic Virus, Infecting Dendrobium Orchid

Plant Disease ◽  
2019 ◽  
Vol 103 (7) ◽  
pp. 1605-1612 ◽  
Author(s):  
Chih-Hung Huang ◽  
Chia-Hsing Tai ◽  
Ruey-Song Lin ◽  
Chung-Jan Chang ◽  
Fuh-Jyh Jan
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Mosaic Virus ◽  
Coat Protein Gene ◽  
Nucleotide Sequence Identity ◽  
Amino Acid Sequence Identity ◽  
Protein Gene ◽  
Sequence Identity

Dendrobium smillieae is one of the popular orchids in Taiwan. This report describes a new potyvirus tentatively named Dendrobium chlorotic mosaic virus (DeCMV) causing chlorotic and mosaic symptoms in D. smillieae. Enzyme-linked immunosorbent assay (ELISA) tests using six antisera against orchid-infecting viruses revealed that only a monoclonal antibody against the potyvirus group reacted positively with crude saps prepared from a symptomatic dendrobium orchid. Potyvirus-like, flexuous, filamentous particles were observed under an electron microscope, measuring approximately 700 to 800 nm in length and 11 to 12 nm in diameter. Sequence analyses revealed that DeCMV coat protein gene shared 59.6 to 66.0% nucleotide sequence identity and 57.6 to 66.0% amino acid sequence identity, whereas the DeCMV complete genome shared 54.1 to 57.3% nucleotide sequence identity and 43.7 to 49.5% amino acid sequence identity with those other known potyviruses. These similarity levels were much lower than the criteria set for species demarcation in potyviruses. Thus, DeCMV can be considered a new potyvirus. The whole DeCMV genome contains 10,041 nucleotides (GenBank accession no. MK241979) and encodes a polyprotein that is predicted to produce 10 proteins by proteolytic cleavage. In a pathogenicity test, results of inoculation assays demonstrated that DeCMV can be transmitted to dendrobium orchids by grafting and mechanical inoculation, as verified by ELISA and western blot analyses using the DeCMV polyclonal antiserum and by reverse transcription polymerase chain reaction using the coat protein gene-specific primers. The inoculated orchids developed similar chlorotic and mosaic symptoms. In conclusion, DeCMV is a novel orchid-infecting potyvirus, and this is the first report of a new potyvirus that infects dendrobium orchids in Taiwan.

scholarly journals Sequence diversity in the coat protein gene of Lettuce big-vein associated virus and Mirafiori lettuce big-vein virus infecting lettuce in Brazil

2008 ◽  
Vol 34 (2) ◽  
pp. 175-177 ◽  
Author(s):  
Márcio Martinello Sanches ◽  
Renate Krause-Sakate ◽  
Marcelo Agenor Pavan
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Coat Protein Gene ◽  
Amino Acid Sequence Identity ◽  
Restriction Site ◽  
Protein Gene ◽  
Sequence Identity ◽  
Disease Analysis ◽  
Vein Disease

Lettuce big vein associated virus (LBVaV) and Mirafiori lettuce big vein virus (MLBVV) have been found in mixed infection in Brazil causing the lettuce big vein disease. Analysis of part of the coat protein (CP) gene of Brazilian isolates of LBVaV collected from lettuce, showed at least 93% amino acid sequence identity with other LBVaV isolates. Genetic diversity among MLBVV CP sequences was higher when compared to LBVaV CP sequences, with amino acid sequence identity ranging between 91% to 100%. Brazilian isolates of MLBVV belong to subgroup A, with one RsaI restriction site on the coat protein gene. There is no indication for a possible geografical origin for the Brazilian isolates of LBVaV and MLBVV.

scholarly journals H-NS Silences gfp, the Green Fluorescent Protein Gene: gfpTCD Is a Genetically Remastered gfp Gene with Reduced Susceptibility to H-NS-Mediated Transcription Silencing and with Enhanced Translation

2010 ◽  
Vol 192 (18) ◽  
pp. 4790-4793 ◽  
Author(s):  
Colin P. Corcoran ◽  
Andrew D. S. Cameron ◽  
Charles J. Dorman
Keyword(s):  
Green Fluorescent Protein ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Reporter Gene ◽  
Protein Gene ◽  
Fluorescent Protein ◽  
Green Fluorescent Protein Gene ◽  
Bacterial Nucleoid ◽  
Green Fluorescent

ABSTRACT The bacterial nucleoid-associated protein H-NS, which preferentially targets and silences A+T-rich genes, binds the ubiquitous reporter gene gfp and dramatically reduces local transcription. We have redesigned gfp to reduce H-NS-mediated transcription silencing and simultaneously improve translation in vivo without altering the amino acid sequence of the GFP protein.

scholarly journals Genetic Mapping of Rabies Virus in Dogs as a Basis for Disease Control

2016 ◽  
Vol 10 (1) ◽  
Author(s):  
Muharam Saepulloh ◽  
R. M. Abdul Adji
Keyword(s):  
Phylogenetic Analysis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phylogenetic Relationship ◽  
Rabies Virus ◽  
Virus Isolate ◽  
Protein Gene ◽  
Genetic Characteristics ◽  
Nucleoprotein Gene ◽  
N Protein

The purpose of this study was to determine the genetic characteristics of rabies virus based on phylogenetic relationship among rabies virus in various regions in Indonesia. The amino acid sequence of the nucleoprotein gene of rabies virus isolate from Banten (RV/Banten01/dog/2007),Makasar (RV/MKS-26/dog/2010), Bukit Tinggi (RV/BKT-52/dog/2009 and RV/BKT-58/dog/2009), Medan (RV/Medan27/dog/2007)andBali(RV/Bali-1/dog/2009;RV/Bali-2/dog/2009;RV/Bali-3/dog/2009),Indonesiawasdetermined.TheseisolatesshowedahighdegreeofhomologyamongIndonesianisolateswhichreached100%.Meanwhile,thelevelofhomologybetweenrabiesvirusisolatesfromcatsrabiesvirusisolatesfromdogsreached97%.ResultsofphylogeneticanalysisusingtheaminoacidsequencesoftheNgenesshowedthatallofIndonesianrabiesvirusisolateswerecloselyrelatedtorabiesvirusesfromChinathanthosefromThailand,Laos,Burma,andVietnamwhichgeograficallycloser to Indonesia. Data obtained from the phylogenetic analysis is expected to trace the source of rabies spread and thepossibility to create a vaccines which more suitable with rabies virus that spreads in Indonesia. Based on the phylogenetic relationship analysisusing the amino acid sequence of the rabies virus N protein gene showed that all of rabies virus isolated from Indonesian regions share a highhomology with others ranging from 97-100%..Key words: sequencing, rabies, nucleoprotein gene (N), homology

scholarly journals ​Cloning and Sequence Analysis of Transferrin Binding Protein Gene A of Field and Vaccine Strains of Pasteurella multocida B:2

2021 ◽  
Author(s):  
Himanshu Sharma ◽  
Y.P. Grover ◽  
Mahavir Singh ◽  
Richa Mishra ◽  
Pankaj Kumar ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Chemical Property ◽  
Vaccine Strain ◽  
Pasteurella Multocida ◽  
Protein Gene ◽  
Physico Chemical ◽  
Binding Protein Gene ◽  
Physico Chemical Property

Background: Pasteurella multocida is an important bacterial pathogen that causes many major diseases of which haemorrhagic septiciemia (HS) in cattle and buffalo is responsible for catastrophic epizootics in India and South Asia. In India, the disease haemorrhagic septiciemia is considered as the most dreaded bacterial disease. Various host- and pathogen- specific determinants are responsible for disease outcome. Various bacterial virulence genes (tbpA, pfhA, toxA, hgbB, hgbA, nanH, nanB, sodA, sodC, oma87 and ptfA) have been proposed to play a key role in this interaction. Methods: The present study was done to compare the gene and deduced amino acid sequence of transferrin binding protein gene (tbpA) gene of field isolates and vaccine strain of P. multocida B: 2. Result: It was observed that tbpA gene of field and vaccine strains have similar nucleotide sequence except at positions 574 and 620. The sequence of tbpA gene was used for prediction of matured TbpA protein characteristics. The deduced amino acid sequences of 242 amino acids revealed 99% homology with TbpA of P. multocida and with a variety of other TonB-dependent receptor proteins, indicating that it belongs to the family of outer membrane receptors. Deduced amino acid sequence was found to be similar in field and vaccine strains except at 207th amino acid. In field isolates Leucine was there while in vaccine strain Phenyl alanine was found. These both amino acids are hydrophobic in nature so no change in physico-chemical property of TbpA is expected. From this study it is concluded that single amino acid difference between field isolate and vaccine strain might not cause change in its binding and physico-chemical property.

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