scholarly journals Biochemical Characterization of theStaphylococcus aureusPcrA Helicase and Its Role in Plasmid Rolling Circle Replication

2002 ◽  
Vol 277 (48) ◽  
pp. 45880-45886 ◽  
Author(s):  
Tseh-Ling Chang ◽  
Asma Naqvi ◽  
Syam P. Anand ◽  
M. Gabriela Kramer ◽  
Rajan Munshi ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Rolling Circle Replication ◽  
Rolling Circle

scholarly journals Characterization of pR18, a novel rolling-circle replication plasmid from Lactobacillus plantarum

Plasmid ◽  
2014 ◽  
Vol 73 ◽  
pp. 1-9 ◽  
Author(s):  
Tannaz Jalilsood ◽  
Ali Baradaran ◽  
Foo Hooi Ling ◽  
Shuhaimi Mustafa ◽  
Khatijah Yusof ◽  
...  
Keyword(s):  
Lactobacillus Plantarum ◽  
Rolling Circle Replication ◽  
Rolling Circle

scholarly journals Genetic and Biochemical Characterization of the Streptococcus pneumoniae PcrA Helicase and Its Role in Plasmid Rolling Circle Replication

2006 ◽  
Vol 188 (21) ◽  
pp. 7416-7425 ◽  
Author(s):  
J. A. Ruiz-Masó ◽  
S. P. Anand ◽  
M. Espinosa ◽  
S. A. Khan ◽  
G. del Solar
Keyword(s):  
Streptococcus Pneumoniae ◽  
Biochemical Characterization ◽  
Essential Gene ◽  
Biochemical Properties ◽  
Dna Helicase ◽  
Rolling Circle Replication ◽  
Lower Efficiency ◽  
Rolling Circle ◽  
Rep Protein

ABSTRACT PcrA is a chromosomally encoded DNA helicase of gram-positive bacteria involved in replication of rolling circle replicating plasmids. Efficient interaction between PcrA and the plasmid-encoded replication initiator (Rep) protein is considered a requirement for the plasmid to replicate in a given host, and thus, the ability of a Rep protein to interact with heterologous PcrA helicases has been invoked as a determinant of plasmid promiscuity. We characterized transcription of the Streptococcus pneumoniae pcrA gene in its genetic context and studied the biochemical properties of its product, the PcrA Spn helicase. Transcription of the pneumococcal pcrA gene was directed by promoter Pa, consisting of an extended −10 box. Promoter Pa also accounted for expression of a second essential gene, radC, which was transcribed with much lower efficiency than pcrA, probably due to the presence of a terminator/attenuator sequence located between the two genes. PcrA Spn displayed single-stranded DNA-dependent ATPase activity. PcrA Spn showed 5′→3′ and 3′→5′ helicase activities and bound efficiently to partially duplex DNA containing a hairpin structure adjacent to a 6-nucleotide 5′ or 3′ single-stranded tail and one unpaired (flap) nucleotide in the complementary strand. PcrA Spn interacted specifically with RepC, the initiator of staphylococcal plasmid pT181. Although the pneumococcal helicase was able to initiate unwinding of the RepC-nicked pT181 DNA, it was much less processive in this activity than the cognate staphylococcal PcrA protein. Accordingly, PcrA Spn was inefficient in in vitro replication of pT181, and perhaps as a consequence, this plasmid could not be established in S. pneumoniae.

Characterization of a Rolling-Circle Replication Plasmid pLR1 from Lactobacillus plantarum LR1

2008 ◽  
Vol 58 (2) ◽  
pp. 106-110 ◽  
Author(s):  
Ruoyu Li ◽  
Zhengyuan Zhai ◽  
Sheng Yin ◽  
Ying Huang ◽  
Qing Wang ◽  
...  
Keyword(s):  
Lactobacillus Plantarum ◽  
Rolling Circle Replication ◽  
Rolling Circle

Characterization of a novel rolling-circle replication plasmid pYSI8 from Lactobacillus sakei YSI8

Plasmid ◽  
2009 ◽  
Vol 62 (1) ◽  
pp. 30-34 ◽  
Author(s):  
Zhengyuan Zhai ◽  
Yanling Hao ◽  
Sheng Yin ◽  
Chunguang Luan ◽  
Liebing Zhang ◽  
...  
Keyword(s):  
Lactobacillus Sakei ◽  
Rolling Circle Replication ◽  
Rolling Circle

scholarly journals Characterization of a rolling-circle replication plasmid from Thermus aquaticus NTU103

Plasmid ◽  
2006 ◽  
Vol 56 (1) ◽  
pp. 46-52 ◽  
Author(s):  
Sheng-Fen Chu ◽  
Hung-Yu Shu ◽  
Ling-Chun Lin ◽  
Mao-Yen Chen ◽  
San-San Tsay ◽  
...  
Keyword(s):  
Rolling Circle Replication ◽  
Thermus Aquaticus ◽  
Rolling Circle

Characterization of three new plasmids from Lactobacillus paracasei 54

2015 ◽  
Vol 40 (3) ◽  
Author(s):  
Xuan Zhu ◽  
Yizhen Zhao ◽  
Chen Zhang ◽  
Lei Shen ◽  
Han Jiang ◽  
...  
Keyword(s):  
Newborn Infant ◽  
Food Industry ◽  
Lactobacillus Paracasei ◽  
Rolling Circle Replication ◽  
Fecal Samples ◽  
Rolling Circle ◽  
Healthy Newborn ◽  
Roche 454

AbstractObjective: Three plasmids from Lactobacillus paracasei 54 were isolated from healthy newborn infant fecal samples.Methods: Plasmid was extracted using an AxyPrep Plasmid Miniprep Kit and lysozyme. The extracted plasmids were sequenced using a Roche 454 Genome Sequencer FLX.Results: Three plasmids were isolated from Lactobacillus paracasei 54. These plasmids are designated pLP5401- 03, and they are 9754, 6650, and 1788 bp in size.Conclusion: Plasmids pLP5401 and pLP5402 were found to contain replication genes that are likely to function via the theta-type mechanism. Plasmid pLP5403 is predicted to replicate via the rolling-circle replication (RCR) mechanism. The RCR replication plasmid can be applied as a useful vector in the food industry

Characterization of a rolling-circle replication plasmid pXY3 from Lactobacillus plantarum XY3

Plasmid ◽  
2010 ◽  
Vol 64 (1) ◽  
pp. 36-40 ◽  
Author(s):  
Hui Zhou ◽  
Yanling Hao ◽  
Ying Xie ◽  
Sheng Yin ◽  
Zhengyuan Zhai ◽  
...  
Keyword(s):  
Lactobacillus Plantarum ◽  
Rolling Circle Replication ◽  
Rolling Circle

scholarly journals Biochemical Characterization of Junonia coenia Densovirus Nonstructural Protein NS-1

2002 ◽  
Vol 76 (1) ◽  
pp. 338-345 ◽  
Author(s):  
Chuantian Ding ◽  
Masashi Urabe ◽  
Max Bergoin ◽  
Robert M. Kotin
Keyword(s):  
Fusion Protein ◽  
Biochemical Characterization ◽  
Nonstructural Protein ◽  
Biochemical Properties ◽  
Junonia Coenia ◽  
Nucleoside Triphosphate ◽  
Rolling Circle Replication ◽  
Structural Protein ◽  
Mobility Shift ◽  
Rolling Circle

ABSTRACT Junonia coenia densovirus (JcDNV) is an autonomous parvovirus that infects the larvae of the common buckeye butterfly, Junonia coenia. Unlike vertebrate parvoviruses, the genes encoding the structural protein and nonstructural (NS) proteins of JcDNV are in opposite orientations; thus, each strand contains a sense and antisense open reading frame (ORF). The promoter at map position 93 controls expression of NS ORFs 2, 3, and 4, which encode three NS proteins, NS-1, NS-2, and NS-3. These proteins are likely to be involved in viral DNA replication, among other functions. In contrast to the nonstructural proteins of the vertebrate parvoviruses, the NS proteins of the Densovirinae have not been characterized. Here, we describe biochemical properties of the NS-1 protein of JcDNV. The NS-1 ORF was cloned in frame with the Escherichia coli malE gene, which encodes the bacterial maltose binding protein (MBP). Using electrophoretic mobility shift and DNase I protection assays, we identified the region of the JcDNV terminal sequence that is recognized specifically by the MBP-NS-1 fusion protein. The site consists of (GAC)4 and is located on the A-A′ region of the terminal palindrome. In addition, the MBP-NS-1 fusion protein catalyzes the cleavage of single-stranded DNA (ssDNA) substrates derived from the JcDNV putative origin of replication, primarily at two sites in the motif 5′-G*TAT*TG-3′. One cleavage site is between the thymidine dinucleotide at positions 92 and 93 and the other site corresponds to thymidine at nucleotide 95; both sites are on the complementary strand of the sequence assigned GenBank accession number A12984 . Cleavage of ssDNA is dependent on the presence of a divalent metal cofactor but does not require nucleoside triphosphate hydrolysis. Parvovirus NS proteins contain the phylogenically conserved Walker A- and B-site ATPase motifs. These sites in JcDNV NS-1 diverge from the consensus, yet despite these atypical motifs our analyses support that MBP-NS-1 has ATP-dependent helicase activity. These results indicate that JcDNV NS-1 possesses activities common to the superfamily of rolling-circle replication initiator proteins in general and the parvovirus replication proteins in particular, and they provide a basis for comparative analyses of the structure and function relationships among the parvovirus NS-1 equivalents.

scholarly journals Characterization of a Staphylococcal Plasmid Related to pUB110 and Carrying Two Novel Genes, vatC andvgbB, Encoding Resistance to Streptogramins A and B and Similar Antibiotics

1998 ◽  
Vol 42 (7) ◽  
pp. 1794-1798 ◽  
Author(s):  
Jeanine Allignet ◽  
Nadia Liassine ◽  
Névine El Solh
Keyword(s):  
Antibiotic Resistance Genes ◽  
Direct Repeats ◽  
Rolling Circle Replication ◽  
Recombination Site ◽  
Site Specific ◽  
Rolling Circle ◽  
Gram Positive Bacteria ◽  
The Common ◽  
Staphylococcus Cohnii

ABSTRACT We isolated and sequenced a plasmid, named pIP1714 (4,978 bp), which specifies resistance to streptogramins A and B and the mixture of these compounds. pIP1714 was isolated from a Staphylococcus cohnii subsp. cohnii strain found in the environment of a hospital where pristinamycin was extensively used. Resistance to both compounds and related antibiotics is encoded by two novel, probably cotranscribed genes, (i) vatC, encoding a 212-amino-acid (aa) acetyltransferase that inactivates streptogramin A and that exhibits 58.2 to 69.8% aa identity with the Vat, VatB, and SatA proteins, and (ii) vgbB, encoding a 295-aa lactonase that inactivates streptogramin B and that shows 67% aa identity with the Vgb lactonase. pIP1714 includes a 2,985-bp fragment also found in two rolling-circle replication and mobilizable plasmids, pUB110 and pBC16, from gram-positive bacteria. In all three plasmids, the common fragment was delimited by two direct repeats of four nucleotides (GGGC) and included (i) putative genes closely related to repB, which encodes a replication protein, and topre(mob), which encodes a protein required for conjugative mobilization and site-specific recombination, and (ii) sequences very similar to the double- and single-strand origins (dso, ssoU ) and the recombination site, RSA. The antibiotic resistance genes repBand pre(mob) carried by each of these plasmids were found in the same transcriptional orientation.

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