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 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

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

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.

Photoinduced DNA cleavage by formation of ROS from oxygen with a neurotransmitter and aromatic amino acids

2010 ◽  
Vol 8 (5) ◽  
pp. 994 ◽  
Author(s):  
Tomonori Kawashima ◽  
Kei Ohkubo ◽  
Shunichi Fukuzumi
Keyword(s):  
Amino Acids ◽  
Dna Cleavage ◽  
Aromatic Amino Acids

scholarly journals The Putative Leucine Zipper of the UL6-Encoded Portal Protein of Herpes Simplex Virus 1 Is Necessary for Interaction with pUL15 and pUL28 and Their Association with Capsids

2009 ◽  
Vol 83 (9) ◽  
pp. 4557-4564 ◽  
Author(s):  
Kui Yang ◽  
Elizabeth Wills ◽  
Joel D. Baines
Keyword(s):  
Amino Acids ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Cleavage ◽  
Leucine Zipper ◽  
Molecular Motor ◽  
Viral Proteins ◽  
Protein Domain ◽  
Portal Protein ◽  
Simplex Virus

ABSTRACT Herpes simplex virus (HSV) type 1 capsids contain a single portal vertex that is composed of 12 copies of the UL6 gene product (pUL6), which forms a pore through which DNA is inserted during packaging. This unique vertex is also believed to comprise the site with which a molecular motor, termed the terminase, associates during the DNA packaging reaction. In HSV, the terminase likely comprises the UL15, UL28, and UL33 proteins (pUL15, pUL28, and pUL33, respectively). The current study was undertaken to identify portal domains required for interaction with the terminase. Both the amino and carboxyl termini, as well as amino acids 422 to 443 of pUL6 forming a putative leucine zipper motif, were critical for coimmunoprecipitation with pUL15 in the absence of other viral proteins. Amino acids 422 to 443 were also necessary for interaction with pUL28 in the absence of other viral proteins. By using an engineered recombinant virus, it was further determined that although amino acids 422 to 443 were dispensable for interaction with scaffold protein and incorporation of portal protein into capsids, they were necessary for coimmunoprecipitation of pUL6 and pUL15 from infected cell lysates, association of optimal levels of pUL15, pUL28, and pUL33 with capsids, and DNA cleavage and packaging. These data identify a portal protein domain critical for terminase association with the capsid and suggest that both the pUL15- and pUL28-bearing terminase subunits mediate docking of the terminase with the portal vertex.

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 Linker Insertion Mutations in the Herpes Simplex Virus Type 1 UL28 Gene: Effects on UL28 Interaction with UL15 and UL33 and Identification of a Second-Site Mutation in the UL15 Gene That Suppresses a Lethal UL28 Mutation

2006 ◽  
Vol 80 (24) ◽  
pp. 12312-12323 ◽  
Author(s):  
Jennie G. Jacobson ◽  
Kui Yang ◽  
Joel D. Baines ◽  
Fred L. Homa
Keyword(s):  
Amino Acids ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Herpes Simplex Virus Type ◽  
Dna Cleavage ◽  
Site Mutation ◽  
Viral Dna ◽  
Simplex Virus ◽  
Insertion Mutants

ABSTRACT The UL28 protein of herpes simplex virus type 1 (HSV-1) is one of seven viral proteins required for the cleavage and packaging of viral DNA. Previous results indicated that UL28 interacts with UL15 and UL33 to form a protein complex (terminase) that is presumed to cleave concatemeric DNA into genome lengths. In order to define the functional domains of UL28 that are important for DNA cleavage/packaging, we constructed a series of HSV-1 mutants with linker insertion and nonsense mutations in UL28. Insertions that blocked DNA cleavage and packaging were found to be located in two regions of UL28: the first between amino acids 200 to 400 and the second between amino acids 600 to 740. Insertions located in the N terminus or in a region located between amino acids 400 and 600 did not affect virus replication. Insertions in the carboxyl terminus of the UL28 protein were found to interfere with the interaction of UL28 with UL33. In contrast, all of the UL28 insertion mutants were found to interact with UL15 but the interaction was reduced with mutants that failed to react with UL33. Together, these observations were consistent with previous conclusions that UL15 and UL33 interact directly with UL28 but interact only indirectly with each other. Revertant viruses that formed plaques on Vero cells were detected for one of the lethal UL28 insertion mutants. DNA sequence analysis, in combination with genetic complementation assays, demonstrated that a second-site mutation in the UL15 gene restored the ability of the revertant to cleave and package viral DNA. The isolation of an intergenic suppressor mutant provides direct genetic evidence of an association between the UL28 and UL15 proteins and demonstrates that this association is essential for DNA cleavage and packaging.

Homochirality as the Signature of Extra-Terrestrial Life

1997 ◽  
Vol 161 ◽  
pp. 505-510
Author(s):  
Alexandra J. MacDermott ◽  
Laurence D. Barron ◽  
Andrè Brack ◽  
Thomas Buhse ◽  
John R. Cronin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Optical Rotation ◽  
Physical Origin ◽  
Natural Choice ◽  
Rosetta Mission ◽  
Terrestrial Life ◽  
Subsurface Layers ◽  
Solar System Bodies ◽  
Origin Of Homochirality

AbstractThe most characteristic hallmark of life is its homochirality: all biomolecules are usually of one hand, e.g. on Earth life uses only L-amino acids for protein synthesis and not their D mirror images. We therefore suggest that a search for extra-terrestrial life can be approached as a Search for Extra- Terrestrial Homochirality (SETH). The natural choice for a SETH instrument is optical rotation, and we describe a novel miniaturized space polarimeter, called the SETH Cigar, which could be used to detect optical rotation as the homochiral signature of life on other planets. Moving parts are avoided by replacing the normal rotating polarizer by multiple fixed polarizers at different angles as in the eye of the bee. We believe that homochirality may be found in the subsurface layers on Mars as a relic of extinct life, and on other solar system bodies as a sign of advanced pre-biotic chemistry. We discuss the chiral GC-MS planned for the Roland lander of the Rosetta mission to a comet and conclude with theories of the physical origin of homochirality.

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