scholarly journals Petunia vein banding virus: Characterization of a New Tymovirus from Petunia × hybrida

Plant Disease ◽  
2000 ◽  
Vol 84 (7) ◽  
pp. 739-742 ◽  
Author(s):  
M. A. V. Alexandre ◽  
L. M. L. Duarte ◽  
E. B. Rivas ◽  
C. M. Chagas ◽  
M. M. Barradas ◽  
...  
Keyword(s):  
Nicotiana Benthamiana ◽  
Petunia Hybrida ◽  
Amino Acid Sequence Identity ◽  
Rio Grande Do Sul ◽  
Cytopathic Effects ◽  
Sequence Identity ◽  
Andean Potato ◽  
Plant Families ◽  
Nicandra Physalodes

Petunia plants from a nursery in the State of Rio Grande do Sul, Brazil, showed pronounced vein banding and contained isometric particles with diameters of approximately 45 and 30 nm. The larger ones apparently represent a caulimovirus, while the smaller ones, which included both empty shells and full particles, were identified as those of a new tymovirus for which we propose the name Petunia vein banding virus (PetVBV). Originally, PetVBV was transmitted only with difficulty to healthy petunia plants. However, from an experimentally infected petu-nia, it was later readily transmitted also to Nicotiana benthamiana and Nicandra physalodes, but not to other species in the Solanaceae or other plant families. It produces cytopathic effects typical for tymovirus infections. Its coat protein shows approximately 65% amino acid sequence identity with those of Eggplant mosaic and Andean potato latent viruses, to which it is also serologically more closely related than to any other tymoviruses.

Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

Biologia ◽  
2011 ◽  
Vol 66 (1) ◽  
Author(s):  
Dessy Natalia ◽  
Keni Vidilaseris ◽  
Pasjan Satrimafitrah ◽  
Wangsa Ismaya ◽  
Purkan ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Saccharomycopsis Fibuligera ◽  
Sequence Identity ◽  
Ic50 Value ◽  
High Amino Acid ◽  
Ph Range

AbstractGlucoamylase from the yeast Saccharomycopsis fibuligera R64 (GLL1) has successfully been purified and characterized. The molecular mass of the enzyme was 56,583 Da as determined by mass spectrometry. The purified enzyme demonstrated optimum activity in the pH range of 5.6–6.4 and at 50°C. The activity of the enzyme was inhibited by acarbose with the IC50 value of 5 μM. GLL1 shares high amino acid sequence identity with GLU1 and GLA1, which are Saccharomycopsis fibuligera glucoamylases from the strains HUT7212 and KZ, respectively. The properties of GLL1, however, resemble that of GLU1. The elucidation of the primary structure of GLL1 contributes to the explanation of this finding.

scholarly journals Nucleotide Sequence and Characterization of a Novel Cefotaxime-Hydrolyzing β-Lactamase (CTX-M-10) Isolated in Spain

2001 ◽  
Vol 45 (2) ◽  
pp. 616-620 ◽  
Author(s):  
Antonio Oliver ◽  
José Claudio Pérez-Dı́az ◽  
Teresa M. Coque ◽  
Fernando Baquero ◽  
Rafael Cantón
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence Identity ◽  
Penicillin G ◽  
Nucleotide Substitutions ◽  
Sequence Identity ◽  
M 10 ◽  
Hydrolysis Rates ◽  
Kluyvera Ascorbata

ABSTRACT A cefotaxime-resistant, ceftazidime-susceptible Escherichia coli isolate was obtained from a patient with sepsis in 1997, from which a β-lactamase with a pI of 8.1 was cloned. Cephaloridine and cefotaxime relative hydrolysis rates were 167 and 81, respectively (penicillin G rate = 100), whereas ceftazidime hydrolysis was not detected. The nucleotide sequence revealed a bla gene related to that coding for CTX-M-3. Despite 21 nucleotide substitutions, only 2 determined amino acid changes (Ala27Val and Arg38Gln). The amino acid sequence identity between this enzyme, designated CTX-M-10, and the chromosomal β-lactamase ofKluyvera ascorbata was 81%.

scholarly journals Genetic and Biochemical Characterization of OXA-535, a Distantly Related OXA-48-Like β-Lactamase

2018 ◽  
Vol 62 (10) ◽  
Author(s):  
L. Dabos ◽  
A. B. Jousset ◽  
R. A. Bonnin ◽  
N. Fortineau ◽  
A. Zavala ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Content Type ◽  
Sequence Identity

ABSTRACT OXA-535 is a chromosome-encoded carbapenemase of Shewanella bicestrii JAB-1 that shares only 91.3% amino acid sequence identity with OXA-48. Catalytic efficiencies are similar to those of OXA-48 for most β-lactams, except for ertapenem, where a 2,000-fold-higher efficiency was observed with OXA-535. OXA-535 and OXA-436, a plasmid-encoded variant of OXA-535 differing by three amino acids, form a novel cluster of distantly related OXA-48-like carbapenemases. Comparison of blaOXA-535 and blaOXA-436 genetic environments suggests that an ISCR1 may be responsible for blaOXA-436 gene mobilization from the chromosome of Shewanella spp. to plasmids.

scholarly journals GS32, a Novel Golgi SNARE of 32 kDa, Interacts Preferentially with Syntaxin 6

1999 ◽  
Vol 10 (1) ◽  
pp. 119-134 ◽  
Author(s):  
Siew Heng Wong ◽  
Yue Xu ◽  
Tao Zhang ◽  
Gareth Griffiths ◽  
Stephen Loucian Lowe ◽  
...  
Keyword(s):  
Amino Acid ◽  
Golgi Apparatus ◽  
Amino Acid Sequence ◽  
Northern Blot Analysis ◽  
Amino Acid Sequence Identity ◽  
Biochemical Characterization ◽  
Polyclonal Antibodies ◽  
Sequence Identity ◽  
Membrane Bound

Syntaxin 1, synaptobrevins or vesicle-associated membrane proteins, and the synaptosome-associated protein of 25 kDa (SNAP-25) are key molecules involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. We report here the molecular, cell biological, and biochemical characterization of a 32-kDa protein homologous to both SNAP-25 (20% amino acid sequence identity) and the recently identified SNAP-23 (19% amino acid sequence identity). Northern blot analysis shows that the mRNA for this protein is widely expressed. Polyclonal antibodies against this protein detect a 32-kDa protein present in both cytosol and membrane fractions. The membrane-bound form of this protein is revealed to be primarily localized to the Golgi apparatus by indirect immunofluorescence microscopy, a finding that is further established by electron microscopy immunogold labeling showing that this protein is present in tubular-vesicular structures of the Golgi apparatus. Biochemical characterizations establish that this protein behaves like a SNAP receptor and is thus named Golgi SNARE of 32 kDa (GS32). GS32 in the Golgi extract is preferentially retained by the immobilized GST–syntaxin 6 fusion protein. The coimmunoprecipitation of syntaxin 6 but not syntaxin 5 or GS28 from the Golgi extract by antibodies against GS32 further sustains the preferential interaction of GS32 with Golgi syntaxin 6.

scholarly journals Characterization of Tbc2, a nucleus-encoded factor specifically required for translation of the chloroplast psbC mRNA in Chlamydomonas reinhardtii

2002 ◽  
Vol 157 (6) ◽  
pp. 953-962 ◽  
Author(s):  
Andrea H. Auchincloss ◽  
William Zerges ◽  
Karl Perron ◽  
Jacqueline Girard-Bascou ◽  
Jean-David Rochaix
Keyword(s):  
Zea Mays ◽  
Amino Acid ◽  
Chlamydomonas Reinhardtii ◽  
Amino Acid Sequence Identity ◽  
Middle Part ◽  
Phenotypic Characterization ◽  
Amino Acid Repeat ◽  
Partial Amino Acid Sequence ◽  
Sequence Identity

Genetic analysis has revealed that the three nucleus-encoded factors Tbc1, Tbc2, and Tbc3 are involved in the translation of the chloroplast psbC mRNA of the eukaryotic green alga Chlamydomonas reinhardtii. In this study we report the isolation and phenotypic characterization of two new tbc2 mutant alleles and their use for cloning and characterizing the Tbc2 gene by genomic complementation. TBC2 encodes a protein of 1,115 residues containing nine copies of a novel degenerate 38–40 amino acid repeat with a quasiconserved PPPEW motif near its COOH-terminal end. The middle part of the Tbc2 protein displays partial amino acid sequence identity with Crp1, a protein from Zea mays that is implicated in the processing and translation of the chloroplast petA and petD RNAs. The Tbc2 protein is enriched in chloroplast stromal subfractions and is associated with a 400-kD protein complex that appears to play a role in the translation of specifically the psbC mRNA.

scholarly journals Cloning and Characterization of a Sulfonate/α-Ketoglutarate Dioxygenase from Saccharomyces cerevisiae

1999 ◽  
Vol 181 (18) ◽  
pp. 5876-5879 ◽  
Author(s):  
Deborah A. Hogan ◽  
Thomas A. Auchtung ◽  
Robert P. Hausinger
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid Sequence Identity ◽  
Ralstonia Eutropha ◽  
Open Reading Frame ◽  
Yeast Protein ◽  
Gene Encoding ◽  
Reading Frame ◽  
Sequence Identity ◽  
Ketoglutarate Dioxygenase

ABSTRACT The Saccharomyces cerevisiae open reading frame YLL057c is predicted to encode a gene product with 31.5% amino acid sequence identity to Escherichia coli taurine/α-ketoglutarate dioxygenase and 27% identity to Ralstonia eutropha TfdA, a herbicide-degrading enzyme. Purified recombinant yeast protein is shown to be an Fe(II)-dependent sulfonate/α-ketoglutarate dioxygenase. Although taurine is a poor substrate, a variety of other sulfonates are utilized, with the best natural substrates being isethionate and taurocholate. Disruption of the gene encoding this enzyme negatively affects the use of isethionate and taurine as sulfur sources byS. cerevisiae, providing strong evidence that YLL057c plays a role in sulfonate catabolism.

scholarly journals Characterization of Class V DyP-Type Peroxidase SaDyP1 from Streptomyces avermitilis and Evaluation of SaDyPs Expression in Mycelium

2021 ◽  
Vol 22 (16) ◽  
pp. 8683
Author(s):  
Kanako Sugawara ◽  
Toru Yoshida ◽  
Rena Hirashima ◽  
Ryoko Toriumi ◽  
Hotaka Akiyama ◽  
...  
Keyword(s):  
Amino Acid Sequence Identity ◽  
Streptomyces Avermitilis ◽  
Wild Type ◽  
Class V ◽  
Anthraquinone Dyes ◽  
Sequence Identity ◽  
High Amino Acid ◽  
Heme Peroxidases ◽  
Optimal Ph

DyP-type peroxidases are a family of heme peroxidases named for their ability to degrade persistent anthraquinone dyes. DyP-type peroxidases are subclassified into three classes: classes P, I and V. Based on its genome sequence, Streptomyces avermitilis, eubacteria, has two genes presumed to encode class V DyP-type peroxidases and two class I genes. We have previously shown that ectopically expressed SaDyP2, a member of class V, indeed has the characteristics of a DyP-type peroxidase. In this study, we analyzed SaDyP1, a member of the same class V as SaDyP2. SaDyP1 showed high amino acid sequence identity to SaDyP2, retaining a conserved GXXDG motif and catalytic aspartate. SaDyP1 degraded anthraquinone dyes, which are specific substrates of DyP-type peroxidases but not azo dyes. In addition to such substrate specificity, SaDyP1 showed other features of DyP-type peroxidases, such as low optimal pH. Furthermore, immunoblotting using an anti-SaDyP2 polyclonal antibody revealed that SaDyP1 and/or SaDyP2 is expressed in mycelia of wild-type S. avermitilis.

scholarly journals Cloning, Expression, and Characterization of a New β-Agarase fromVibriosp. Strain CN41

2011 ◽  
Vol 77 (19) ◽  
pp. 7077-7079 ◽  
Author(s):  
Li Liao ◽  
Xue-Wei Xu ◽  
Xia-Wei Jiang ◽  
Yi Cao ◽  
Na Yi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glycoside Hydrolase ◽  
Amino Acid Sequence Identity ◽  
Sequence Identity

ABSTRACTA new agarase, AgaACN41, cloned fromVibriosp. strain CN41, consists of 990 amino acids, with only 49% amino acid sequence identity with known β-agarases. AgaACN41belongs to the GH50 (glycoside hydrolase 50) family but yields neoagarotetraose as the end product. AgaACN41was expressed and characterized.

scholarly journals A novel homologue of Human herpesvirus 6 in chimpanzees

2005 ◽  
Vol 86 (8) ◽  
pp. 2135-2140 ◽  
Author(s):  
Vincent Lacoste ◽  
Ernst J. Verschoor ◽  
Eric Nerrienet ◽  
Antoine Gessain
Keyword(s):  
Sequence Variation ◽  
Amino Acid Sequence Identity ◽  
Human Herpesvirus ◽  
Viral Sequence ◽  
Human Herpesvirus 6 ◽  
Sequence Identity ◽  
Viral Transactivator ◽  
Pcr Method ◽  
Herpesvirus 6

Among the Betaherpesvirinae, human cytomegalovirus is the only virus to possess simian homologues. Indeed, intriguingly, no close simian homologue of the roseoloviruses Human herpesvirus 6 (HHV-6) and Human herpesvirus 7 (HHV-7), the other two human members of the Betaherpesvirinae, has been identified to date. Here, the first simian homologue of HHV-6 is described, which was identified in common chimpanzees and designated PanHV6. By using a degenerate consensus PCR method, three different gene fragments were amplified, corresponding to the DNA polymerase (U38), β-chemokine receptor (U12) and viral transactivator (U42) genes, with 94–96 % (nucleotide) and 95–97 % (amino acid) sequence identity to the corresponding genes of HHV-6B. Analysis of 77 predominantly wild-caught chimpanzees identified a unique PanHV6 strain in 21 animals, with no viral sequence variation between the different chimpanzee subspecies that were found to be infected. Characterization of this virus represents a great potential to gain a better understanding of the diseases associated with HHV-6.

scholarly journals Revision of the Nomenclature for the Bacillus thuringiensis Pesticidal Crystal Proteins

1998 ◽  
Vol 62 (3) ◽  
pp. 807-813 ◽  
Author(s):  
N. Crickmore ◽  
D. R. Zeigler ◽  
J. Feitelson ◽  
E. Schnepf ◽  
J. Van Rie ◽  
...  
Keyword(s):  
Amino Acid ◽  
Bacillus Thuringiensis ◽  
Amino Acid Sequence Identity ◽  
Crystal Protein ◽  
Nomenclature System ◽  
Sequence Identity ◽  
Crystal Proteins ◽  
Ranking Criterion ◽  
Rapid Characterization

SUMMARY The crystal proteins of Bacillus thuringiensis have been extensively studied because of their pesticidal properties and their high natural levels of production. The increasingly rapid characterization of new crystal protein genes, triggered by an effort to discover proteins with new pesticidal properties, has resulted in a variety of sequences and activities that no longer fit the original nomenclature system proposed in 1989. Bacillus thuringiensis pesticidal crystal protein (Cry and Cyt) nomenclature was initially based on insecticidal activity for the primary ranking criterion. Many exceptions to this systematic arrangement have become apparent, however, making the nomenclature system inconsistent. Additionally, the original nomenclature, with four activity-based primary ranks for 13 genes, did not anticipate the current 73 holotype sequences that form many more than the original four subgroups. A new nomenclature, based on hierarchical clustering using amino acid sequence identity, is proposed. Roman numerals have been exchanged for Arabic numerals in the primary rank (e.g., Cry1Aa) to better accommodate the large number of expected new sequences. In this proposal, 133 crystal proteins comprising 24 primary ranks are systematically arranged.

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