scholarly journals Study on characterization of chalcone synthase gene from \(\textit{Pueraria lobata}\) and \(\textit{Pueraria mirifica}\) in Vietnam

2021 ◽  
Vol 43 (3) ◽  
pp. 47-58
Author(s):  
Huynh Thi Thu Hue ◽  
Nguyen Minh Phuong ◽  
Nguyen Xuan Canh
Keyword(s):  
Chalcone Synthase ◽  
Stilbene Synthase ◽  
Pueraria Lobata ◽  
Pueraria Mirifica ◽  
Reading Frame ◽  
Chalcone Synthase Gene ◽  
The Family ◽  
Ancient Times ◽  
And Function

Two species of genus Pueraria ((Pueraria lobata (synonym: Pueraria montana var. lobata) and Pueraria mirifica (synonym: Pueraria candollei var. mirifica)) are traditional plants used in medicine since ancient times. These plants have been used and became commercially crucial indigenous medicinal plants. Currently, both roots and flowers of P. mirifica are used as a dietary supplement and functional food for women because of their rich source of phytoestrogen and nutrition. However, little information of genes on both species of Pueraria genus (P. lobata and P. mirifica) are known in Vietnam. The purpose of this research is to support more understanding about Chalcone synthase (CHS) genes by determining and sequence analyzing an encoding region of CHS genes that were isolated from P. lobata and P. mirifica. The full-length open reading frame (ORF) sequence CHS was identified with 1170 bp which encodes 389 amino acids by Sanger sequencing. The isolated CHS gene of P. lobata has no difference in sequence with CHS reported on GenBank (D10223.1), whereas a difference of 26 nucleotide positions in CHS sequence of P. mirifica compared with the published gene sequence (JQ409456.1) as consequential having  97.78% genetic similarity. The CHS genes sequence of P. lobata and P. mirifica are homologous with 98.4% because of having 19 nucleotide differences. Chalcone-stilbene synthase N-C terminal, PLN03173, CHS-like, BH0617, fabH are some important domains predicting the CHS genes. Especially, the family signature ‘GVLFGFGPGLTI’ motif of CHS gene as a part of the active-site scaffold contributes to decide the product of cyclization reactions performing the stereochemistry of cyclization which was also observed in P. lobata and P. mirifica, but it was not included for all members in Fabaceae family. With in sillico analysis, the P. lobata and P. mirifica CHS sequences have highly conserved regions to maintain their structure and function, so that it needs further studies to clarify these points.

scholarly journals Functional Diversity among Metallo-β-Lactamases: Characterization of the CAR-1 Enzyme of Erwinia carotovora

2008 ◽  
Vol 52 (7) ◽  
pp. 2473-2479 ◽  
Author(s):  
Magdalena Stoczko ◽  
Jean-Marie Frère ◽  
Gian Maria Rossolini ◽  
Jean-Denis Docquier
Keyword(s):  
Functional Diversity ◽  
Clinical Importance ◽  
Erwinia Carotovora ◽  
Exchange Chromatography ◽  
Genome Database ◽  
Reading Frame ◽  
The Family ◽  
Functional Features ◽  
Hydrolysis Of

ABSTRACT Metallo-β-lactamases (MBLs) are zinc-dependent bacterial enzymes characterized by an efficient hydrolysis of carbapenems and a lack of sensitivity to commercially available β-lactamase inactivators. Apart from the acquired subclass B1 enzymes, which exhibit increasing clinical importance and whose evolutionary origin remains unclear, most MBLs are encoded by resident genes found in the genomes of organisms belonging to at least three distinct phyla. Using genome database mining, we identified an open reading frame (ORF) (ECA2849) encoding an MBL-like protein in the sequenced genome of Erwinia carotovora, an important plant pathogen. Although no detectable β-lactamase activity could be found in E. carotovora, a recombinant Escherichia coli strain in which the ECA2849 ORF was cloned showed decreased susceptibility to several β-lactams, while carbapenem MICs were surprisingly poorly affected. The enzyme, named CAR-1, was purified by means of ion-exchange chromatography steps, and its characterization revealed unique structural and functional features. This new MBL was able to efficiently hydrolyze cephalothin, cefuroxime, and cefotaxime and, to a lesser extent, penicillins and the other cephalosporins but only poorly hydrolyzed meropenem, while imipenem was not recognized. CAR-1 is the first example of a functional naturally occurring MBL in the family Enterobacteriaceae (order Enterobacteriales) and highlights the extraordinary structural and functional diversity exhibited by MBLs.

scholarly journals Isolation and Characterization of an Arterivirus Defective Interfering RNA Genome

2000 ◽  
Vol 74 (7) ◽  
pp. 3156-3165 ◽  
Author(s):  
Richard Molenkamp ◽  
Babette C. D. Rozier ◽  
Sophie Greve ◽  
Willy J. M. Spaan ◽  
Eric J. Snijder
Keyword(s):  
Rna Virus ◽  
Equine Arteritis Virus ◽  
Reading Frame ◽  
Isolation And Characterization ◽  
The Family ◽  
Defective Interfering Rna ◽  
Rna Genome ◽  
Interfering Rna ◽  
Discontinuous Transcription

ABSTRACT Equine arteritis virus (EAV), the type member of the family Arteriviridae, is a single-stranded RNA virus with a positive-stranded genome of approximately 13 kb. EAV uses a discontinuous transcription mechanism to produce a nested set of six subgenomic mRNAs from which its structural genes are expressed. We have generated the first documented arterivirus defective interfering (DI) RNAs by serial undiluted passaging of a wild-type EAV stock in BHK-21 cells. A cDNA copy of the smallest DI RNA (5.6 kb) was cloned. Upon transfection into EAV-infected BHK-21 cells, transcripts derived from this clone (pEDI) were replicated and packaged. Sequencing of pEDI revealed that the DI RNA was composed of three segments of the EAV genome (nucleotides 1 to 1057, 1388 to 1684, and 8530 to 12704) which were fused in frame with respect to the replicase reading frame. Remarkably, this DI RNA has retained all of the sequences encoding the structural proteins. By insertion of the chloramphenicol acetyltransferase reporter gene in the DI RNA genome, we were able to delimitate the sequences required for replication/DI-based transcription and packaging of EAV DI RNAs and to reduce the maximal size of a replication-competent EAV DI RNA to approximately 3 kb.

scholarly journals Sequencing of the rpoB Gene inLegionella pneumophila and Characterization of Mutations Associated with Rifampin Resistance in theLegionellaceae

2000 ◽  
Vol 44 (10) ◽  
pp. 2679-2683 ◽  
Author(s):  
K. Nielsen ◽  
P. Hindersson ◽  
N. Høiby ◽  
J. M. Bangsborg
Keyword(s):  
Dna Sequence ◽  
Legionella Pneumophila ◽  
Resistance Mechanism ◽  
Rpob Gene ◽  
Single Strain ◽  
Reading Frame ◽  
Recommended Treatment ◽  
The Family ◽  
Rifampin Resistance

ABSTRACT Rifampin in combination with erythromycin is a recommended treatment for severe cases of legionellosis. Mutations in therpoB gene are known to cause rifampin resistance inEscherichia coli and Mycobacterium tuberculosis, and the purpose of the present study was to investigate a possible similar resistance mechanism within the members of the family Legionellaceae. Since the RNA polymerase genes of this genus have never been characterized, the DNA sequence of the Legionella pneumophila rpoB gene was determined by the Vectorette technique for genome walking. A 4,647-bp DNA sequence that contained the open reading frame (ORF) of the rpoB gene (4,104 bp) and an ORF of 384 bp representing part of therpoC gene was obtained. A 316-bp DNA fragment in the center of the L. pneumophila rpoB gene, corresponding to a previously described site for mutations leading to rifampin resistance in M. tuberculosis, was sequenced from 18 rifampin-resistant Legionella isolates representing four species (L. bozemanii, L. longbeachae, L. micdadei, and L. pneumophila), and the sequences were compared to the sequences of the fragments from the parent (rifampin-sensitive) strains. Six single-base mutations which led to amino acid substitutions at five different positions were identified. A single strain did not contain any mutations in the 316-bp fragment. This study represents the characterization of a hitherto undescribed resistance mechanism within the family Legionellaceae.

Cloning and characterization of a novel chalcone synthase gene from Phalaenopsis hybrida orchid flowers

2006 ◽  
Vol 53 (2) ◽  
pp. 223-230 ◽  
Author(s):  
Y. Y. Han ◽  
F. Ming ◽  
J. W. Wang ◽  
J. G. Wen ◽  
M. M. Ye ◽  
...  
Keyword(s):  
Chalcone Synthase ◽  
Chalcone Synthase Gene ◽  
Phalaenopsis Hybrida

Cloning and Characterization of Chalcone Synthase Gene from Pueraria candollei var. mirifica

2010 ◽  
Vol 150 ◽  
pp. 478-478
Author(s):  
Piyachat Wiriyaampaiwong ◽  
Pornthap Thanonkeo ◽  
Sudarat Thanonkeo
Keyword(s):  
Chalcone Synthase ◽  
Pueraria Candollei ◽  
Chalcone Synthase Gene

Identification and Characterization of Chalcone Synthase Gene Family Members in Nicotiana tabacum

2016 ◽  
Vol 36 (2) ◽  
pp. 374-384 ◽  
Author(s):  
Shuai Chen ◽  
Xuhao Pan ◽  
Yiting Li ◽  
Lijie Cui ◽  
Yinchao Zhang ◽  
...  
Keyword(s):  
Nicotiana Tabacum ◽  
Gene Family ◽  
Chalcone Synthase ◽  
Family Members ◽  
Chalcone Synthase Gene ◽  
Identification And Characterization

scholarly journals Natural Transformation in Mesophilic and Thermophilic Bacteria: Identification and Characterization of Novel, Closely Related Competence Genes in Acinetobacter sp. Strain BD413 andThermus thermophilus HB27

2001 ◽  
Vol 67 (7) ◽  
pp. 3140-3148 ◽  
Author(s):  
Alexandra Friedrich ◽  
Thomas Hartsch ◽  
Beate Averhoff
Keyword(s):  
Natural Transformation ◽  
Thermophilic Bacteria ◽  
Thermus Thermophilus ◽  
Kanamycin Resistance ◽  
Amino Acid Sequences ◽  
Reading Frame ◽  
Competence Proteins ◽  
And Function ◽  
Product Displays

ABSTRACT The mesophile Acinetobacter sp. strain BD413 and the extreme thermophile Thermus thermophilus HB27 display high frequencies of natural transformation. In this study we identified and characterized a novel competence gene in Acinetobacter sp. strain BD413, comA, whose product displays significant similarities to the competence proteins ComA and ComEC inNeisseria and Bacillus species. Transcription of comA correlated with growth phase-dependent transcriptional regulation of the recently identified pilin-like factors of the transformation machinery. This finding strongly suggests that comA is part of a competence regulon. Examination of the genome sequence of T. thermophilus HB27 led to detection of a comA/comEC-like open reading frame (ORF) which is flanked by an ORF whose product shows significant similarities to the Bacillus subtilis competence protein ComEA. To examine whether these two ORFs, designated comEC andcomEA, are implicated in natural transformation of T. thermophilus HB27, both were disrupted by using a thermostable kanamycin resistance marker. Natural transformation in comEC mutants was reduced 1,000-fold, whereas in comEA mutants the natural transformation phenotype was completely eliminated. These results strongly suggest that both genes, comEC and comEA, are required for natural transformation in T. thermophilus HB27. Several transmembrane α-helices are predicted based on the amino acid sequences of ComA in Acinetobacter sp. strain BD413 and ComEC in T. thermophilus HB27, which suggests that ComA and ComEC are located in the inner membrane and function in DNA transport through the cytoplasmic membrane.

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