scholarly journals Conjugative transposition of the vancomycin resistance carrying Tn1549: enzymatic requirements and target site preferences

2018 ◽  
Vol 107 (5) ◽  
pp. 639-658 ◽  
Author(s):  
Lotte Lambertsen ◽  
Anna Rubio-Cosials ◽  
Kiran Raosaheb Patil ◽  
Orsolya Barabas
Keyword(s):  
Vancomycin Resistance ◽  
Target Site ◽  
Site Preferences ◽  
Conjugative Transposition

scholarly journals DNA Integration by Ty Integrase in yku70Mutant Saccharomyces cerevisiae Cells

2000 ◽  
Vol 20 (23) ◽  
pp. 8836-8844 ◽  
Author(s):  
Markus Kiechle ◽  
Anna A. Friedl ◽  
Palaniyandi Manivasakam ◽  
Friederike Eckardt-Schupp ◽  
Robert H. Schiestl
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasmid Dna ◽  
Integration Site ◽  
Cellular Function ◽  
Target Site ◽  
Target Site Duplication ◽  
Wild Type ◽  
Dna Integration ◽  
Site Preferences

ABSTRACT In the present work we examined nonhomologous integration of plasmid DNA in a yku70 mutant. Ten of 14 plasmids integrated as composite elements, including Ty sequences probably originating from erroneous strand-switching and/or priming events. Three additional plasmids integrated via Ty integrase without cointegrating Ty sequences, as inferred from 5-bp target site duplication and integration site preferences. Ty integrase-mediated integration of non-Ty DNA has never been observed in wild-type cells, although purified integrase is capable of using non-Ty DNA as a substrate in vitro. Hence our data implicate yKu70 as the cellular function preventing integrase from accepting non-Ty DNA as a substrate.

Target-site Preferences of Sleeping Beauty Transposons

2005 ◽  
Vol 346 (1) ◽  
pp. 161-173 ◽  
Author(s):  
Geyi Liu ◽  
Aron M. Geurts ◽  
Kojiro Yae ◽  
A.R. Srinivasan ◽  
Scott C. Fahrenkrug ◽  
...  
Keyword(s):  
Sleeping Beauty ◽  
Target Site ◽  
Site Preferences

scholarly journals Use of Patient-Derived Human Immunodeficiency Virus Type 1 Integrases To Identify a Protein Residue That Affects Target Site Selection

2001 ◽  
Vol 75 (16) ◽  
pp. 7756-7762 ◽  
Author(s):  
Amy L. Harper ◽  
Lynn M. Skinner ◽  
Malgorzata Sudol ◽  
Michael Katzman
Keyword(s):  
Human Immunodeficiency Virus ◽  
Amino Acid ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Target Site ◽  
Site Preferences ◽  
Immunodeficiency Virus ◽  
Cellular Dna ◽  
Hiv 1

ABSTRACT To identify parts of retroviral integrase that interact with cellular DNA, we tested patient-derived human immunodeficiency virus type 1 (HIV-1) integrases for alterations in the choice of nonviral target DNA sites. This strategy took advantage of the genetic diversity of HIV-1, which provided 75 integrase variants that differed by a small number of amino acids. Moreover, our hypothesis that biological pressures on the choice of nonviral sites would be minimal was validated when most of the proteins that catalyzed DNA joining exhibited altered target site preferences. Comparison of the sequences of proteins with the same preferences then guided mutagenesis of a laboratory integrase. The results showed that single amino acid substitutions at one particular residue yielded the same target site patterns as naturally occurring integrases that included these substitutions. Similar results were found with DNA joining reactions conducted with Mn2+ or with Mg2+ and were confirmed with a nonspecific alcoholysis assay. Other amino acid changes at this position also affected target site preferences. Thus, this novel approach has identified a residue in the central domain of HIV-1 integrase that interacts with or influences interactions with cellular DNA. The data also support a model in which integrase has distinct sites for viral and cellular DNA.

scholarly journals Retroviral DNA Integration: ASLV, HIV, and MLV Show Distinct Target Site Preferences

PLoS Biology ◽  
2004 ◽  
Vol 2 (8) ◽  
pp. e234 ◽  
Author(s):  
Rick S Mitchell ◽  
Brett F Beitzel ◽  
Astrid R. W Schroder ◽  
Paul Shinn ◽  
Huaming Chen ◽  
...  
Keyword(s):  
Target Site ◽  
Dna Integration ◽  
Site Preferences

scholarly journals An Amino Acid in the Central Catalytic Domain of Three Retroviral Integrases That Affects Target Site Selection in Nonviral DNA

2003 ◽  
Vol 77 (6) ◽  
pp. 3838-3845 ◽  
Author(s):  
Amy L. Harper ◽  
Malgorzata Sudol ◽  
Michael Katzman
Keyword(s):  
Amino Acid ◽  
Catalytic Domain ◽  
Target Site ◽  
Rous Sarcoma ◽  
Site Preferences ◽  
Target Dna ◽  
Sarcoma Virus ◽  
Cellular Dna

ABSTRACT Integrase can insert retroviral DNA into almost any site in cellular DNA; however, target site preferences are noted in vitro and in vivo. We recently demonstrated that amino acid 119, in the α2 helix of the central domain of the human immunodeficiency virus type 1 integrase, affected the choice of nonviral target DNA sites. We have now extended these findings to the integrases of a nonprimate lentivirus and a more distantly related alpharetrovirus. We found that substitutions at the analogous positions in visna virus integrase and Rous sarcoma virus integrase changed the target site preferences in five assays that monitor insertion into nonviral DNA. Thus, the importance of this protein residue in the selection of nonviral target DNA sites is likely to be a general property of retroviral integrases. Moreover, this amino acid might be part of the cellular DNA binding site on integrase proteins.

scholarly journals Target Site Preferences of Subgroup C Rous Sarcoma Virus Integration into the Chicken DNA

2008 ◽  
Vol 1 (1) ◽  
pp. 6-12 ◽  
Author(s):  
Marketa Reinisova ◽  
Adam Pavlicek ◽  
Petr Divina ◽  
Josef Geryk ◽  
Jiri Plachy ◽  
...  
Keyword(s):  
Rous Sarcoma Virus ◽  
Target Site ◽  
Rous Sarcoma ◽  
Site Preferences ◽  
Sarcoma Virus ◽  
Virus Integration

Molecular Characterization of Methicillin Resistant and Extended Spectrum β-Lactamase Staphylococcus aureus Isolated from Burn Patients

2020 ◽  
pp. 145-151
Author(s):  
Shawnm Ahmed Aziz
Keyword(s):  
Staphylococcus Aureus ◽  
Methicillin Resistance ◽  
Vancomycin Resistance ◽  
World Health ◽  
Molecular Technique ◽  
Burn Patients ◽  
Beta Lactamase ◽  
Beta Lactam ◽  
Extended Spectrum Beta Lactamase ◽  
Extended Spectrum

Antibiotic resistance has become a major world health challenge and has limited the ability of physician's treatment. Staphylococcus aureus the most notorious pathogens causes morbidity and mortality especially in burn patients. However, Staphylococcus aureus rapidly acquired resistance to multiple antibiotics. Vancomycin, a glycopeptide antibiotic remains a drug of choice for treatment of severe Methicillin Resistance S. aureus infections. This study aimed to detect the emergence of beta-lactam and glycopeptide resistance genes. 50 clinical specimens of S. aureus collected from burn patients in burn and plastic surgery units in Sulaimani-Iraq city. All specimens were confirmed to be positive for S. aureus. All the isolates were assessed for their susceptibility to different antibiotics depending on NCCL standards, followed by Extended Spectrum Beta Lactamase detection by double disk diffusion synergy test. The production of β- lactamases was evaluated in the isolated strains by several routine methods and polymerase chain reaction. Among the isolates 94% were Methicillin resistance and 34.28% were Extended Spectrum Beta Lactamase producer. PCR based molecular technique was done for the bla genes related to β- lactamase enzymes by the specific primers, as well as genes which related to reduced sensitivity to Vancomycin were detected. The results indicated that all isolated showed the PBP1, PBP2, PBP3, PBP4, trfA and trfB, graSR, vraS except the vraR gene and the prolonged therapy of Methicillin resistance infection with teicoplanin have been associated with progress of resistance and the rise of tecoplanin resistance may be a prologue to evolving Vancomycin resistance. In conclusion, beta-lactam over taking can rise Vancomycin- Intermediate S. aureus strains leading to appearance of Vancomycin resistance although the treatment of Vancomycin resistant infections is challenging.

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