DNA Cleavage by New Oxovanadium(IV) Complexes ofN-Salicylidene α-Amino Acids and Phenanthroline Bases in the Photodynamic Therapy Window

2007 ◽  
Vol 46 (26) ◽  
pp. 11112-11121 ◽  
Author(s):  
Pijus K. Sasmal ◽  
Ashis K. Patra ◽  
Munirathinam Nethaji ◽  
Akhil R. Chakravarty
Keyword(s):  
Amino Acids ◽  
Photodynamic Therapy ◽  
Dna Cleavage ◽  
Phenanthroline Bases

DNA cleavage in red light promoted by copper(ii) complexes of α-amino acids and photoactive phenanthroline bases

2008 ◽  
pp. 6966 ◽  
Author(s):  
Ashis K. Patra ◽  
Tuhin Bhowmick ◽  
Suryanarayanarao Ramakumar ◽  
Munirathinam Nethaji ◽  
Akhil R. Chakravarty
Keyword(s):  
Amino Acids ◽  
Dna Cleavage ◽  
Red Light ◽  
Phenanthroline Bases

scholarly journals A Domain of Herpes Simplex Virus pUL33 Required To Release Monomeric Viral Genomes from Cleaved Concatemeric DNA

2017 ◽  
Vol 91 (20) ◽  
Author(s):  
Kui Yang ◽  
Xiaoqun Dang ◽  
Joel D. Baines
Keyword(s):  
Amino Acids ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Viral Replication ◽  
Dna Cleavage ◽  
Artificial Chromosome ◽  
Viral Dna ◽  
Viral Genomes ◽  
C Terminus ◽  
Simplex Virus

ABSTRACT Monomeric herpesvirus DNA is cleaved from concatemers and inserted into preformed capsids through the actions of the viral terminase. The terminase of herpes simplex virus (HSV) is composed of three subunits encoded by UL15, UL28, and UL33. The UL33-encoded protein (pUL33) interacts with pUL28, but its precise role in the DNA cleavage and packaging reaction is unclear. To investigate the function of pUL33, we generated a panel of recombinant viruses with either deletions or substitutions in the most conserved regions of UL33 using a bacterial artificial chromosome system. Deletion of 11 amino acids (residues 50 to 60 or residues 110 to 120) precluded viral replication, whereas the truncation of the last 10 amino acids from the pUL33 C terminus did not affect viral replication or the interaction of pUL33 with pUL28. Mutations that replaced the lysine at codon 110 and the arginine at codon 111 with alanine codons failed to replicate, and the pUL33 mutant interacted with pUL28 less efficiently. Interestingly, genomic termini of the large (L) and small (S) components were detected readily in cells infected with these mutants, indicating that concatemeric DNA was cleaved efficiently. However, the release of monomeric genomes as assessed by pulsed-field gel electrophoresis was greatly diminished, and DNA-containing capsids were not observed. These results suggest that pUL33 is necessary for one of the two viral DNA cleavage events required to release individual genomes from concatemeric viral DNA. IMPORTANCE This paper shows a role for pUL33 in one of the two DNA cleavage events required to release monomeric genomes from concatemeric viral DNA. This is the first time that such a phenotype has been observed and is the first identification of a function of this protein relevant to DNA packaging other than its interaction with other terminase components.

Synthesis and DNA cleavage properties of ternary Cu(II) complexes containing histamine and amino acids

2006 ◽  
Vol 47 (41) ◽  
pp. 7311-7315 ◽  
Author(s):  
Pulimamidi Rabindra Reddy ◽  
Kandibanda Srinivasa Rao ◽  
Battu Satyanarayana
Keyword(s):  
Amino Acids ◽  
Dna Cleavage

Tumor microenvironment-responsive charge reversal zinc phthalocyanines based on amino acids for photodynamic therapy

2016 ◽  
Vol 126 ◽  
pp. 239-250 ◽  
Author(s):  
Ao Wang ◽  
Li Gui ◽  
Shan Lu ◽  
Lin Zhou ◽  
Jiahong Zhou ◽  
...  
Keyword(s):  
Amino Acids ◽  
Photodynamic Therapy ◽  
Tumor Microenvironment ◽  
Charge Reversal ◽  
Zinc Phthalocyanines

Photocytotoxicity and DNA cleavage activity of l-arg and l-lys Schiff base oxovanadium(iv) complexes having phenanthroline bases

2010 ◽  
Vol 39 (30) ◽  
pp. 7104 ◽  
Author(s):  
Pijus K. Sasmal ◽  
Ritankar Majumdar ◽  
Rajan R. Dighe ◽  
Akhil R. Chakravarty
Keyword(s):  
Schiff Base ◽  
Dna Cleavage ◽  
Cleavage Activity ◽  
Dna Cleavage Activity ◽  
Phenanthroline Bases

scholarly journals Phosphorus (V) porphyrin diaxially substituted with Leu-enkephalin

2004 ◽  
Vol 2 (3) ◽  
pp. 446-455 ◽  
Author(s):  
Mariusz Gajewski ◽  
Leszek Czuchajowski
Keyword(s):  
Amino Acids ◽  
Photodynamic Therapy ◽  
Amino Acid ◽  
Biologically Active ◽  
Solution Phase ◽  
Terminal Amino Acid ◽  
Leucine Enkephalin ◽  
Potential Applications ◽  
Biologically Active Peptide ◽  
Terminal Amino

AbstractSynthesis of the first phosphorus (V) porphyrin-peptide conjugate was successfully accomplished. A biologically active peptide, leucine enkephalin, was constructed on the phosphorus atom of the 5,10,15,20-meso-tetraphenylporphinato dichlorophosphorus (V) chloride. The method involved solution phase peptide synthesis. The first C-terminal amino acid in the sequence of the peptide was axially attached to the porphyrin through a linker, 3-aminopropanol, and the remainder of leucine enkephalin was synthesized by subsequent additions of amino acids. Leucine enkephalin-P(V) porphyrin conjugate represents a new group of compounds, and its synthesis broadens potential applications of P(V) porphyrine, e.g. in photodynamic therapy.

Anaerobic DNA cleavage activity in red light and photocytotoxicity of (pyridine-2-thiol)cobalt(iii) complexes of phenanthroline bases

2010 ◽  
Vol 39 (7) ◽  
pp. 1807 ◽  
Author(s):  
Debojyoti Lahiri ◽  
Sovan Roy ◽  
Sounik Saha ◽  
Ritankar Majumdar ◽  
Rajan R. Dighe ◽  
...  
Keyword(s):  
Dna Cleavage ◽  
Red Light ◽  
Cleavage Activity ◽  
Dna Cleavage Activity ◽  
Phenanthroline Bases

Photosensitized DNA cleavage promoted by amino acids

2003 ◽  
pp. 1956-1957 ◽  
Author(s):  
Kerry P. Mahon, Jr. ◽  
Rodrigo F. Ortiz-Meoz ◽  
Erin G. Prestwich ◽  
Shana O. Kelley
Keyword(s):  
Amino Acids ◽  
Dna Cleavage

scholarly journals Role of the UL25 Protein in Herpes Simplex Virus DNA Encapsidation

2008 ◽  
Vol 83 (1) ◽  
pp. 47-57 ◽  
Author(s):  
Shelley K. Cockrell ◽  
Minerva E. Sanchez ◽  
Angela Erazo ◽  
Fred L. Homa
Keyword(s):  
Amino Acids ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Cleavage ◽  
Virus Protein ◽  
Viral Dna ◽  
Reading Frame ◽  
Viral Genomes ◽  
Simplex Virus

ABSTRACT The herpes simplex virus protein UL25 attaches to the external vertices of herpes simplex virus type 1 capsids and is required for the stable packaging of viral DNA. To define regions of the protein important for viral replication and capsid attachment, the 580-amino-acid UL25 open reading frame was disrupted by transposon mutagenesis. The UL25 mutants were assayed for complementation of a UL25 deletion virus, and in vitro-synthesized protein was tested for binding to UL25-deficient capsids. Of the 11 mutants analyzed, 4 did not complement growth of the UL25 deletion mutant, and analysis of these and additional mutants in the capsid-binding assay demonstrated that UL25 amino acids 1 to 50 were sufficient for capsid binding. Several UL25 mutations were transferred into recombinant viruses to analyze the effect of the mutations on UL25 capsid binding and on DNA cleavage and packaging. Studies of these mutants demonstrated that amino acids 1 to 50 of UL25 are essential for its stable interaction with capsids and that the C terminus is essential for DNA packaging and the production of infectious virus through its interactions with other viral packaging or tegument proteins. Analysis of viral DNA cleavage demonstrated that in the absence of a functional UL25 protein, aberrant cleavage takes place at the unique short end of the viral genome, resulting in truncated viral genomes that are not retained in capsids. Based on these observations, we propose a model where UL25 is required for the formation of DNA-containing capsids by acting to stabilize capsids that contain full-length viral genomes.

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