The terminal regions of adenovirus and minute virus of mice DNAs are preferentially associated with the nuclear matrix in infected cells

Bodnar, John W.; Hanson, Phyllis I.; Polvino-Bodnar, Maryellen; Zempsky, W; Ward, David C.

doi:10.1128/jvi.63.10.4344-4353.1989

Cited by 46 publications

(19 citation statements)

References 69 publications

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“…Sall, which incised a site three bases from the ClAde substitution, cleaved the modified strand half as well as it did the normal strand. Our results are similar to those by Bodnar and co-workers (21) in which structural alterations in a base pair immediately adjacent to bonds cleaved by an enzyme reduced the rate of cleavage most dramatically. Only one enyzme examined thus far, Narl, consistently hydrolyzed ClAde-containing duplex DNA to a greater extent than it did Ade-containing sites.…”

Section: Results and Discussion Synthesis Of 'Clade'-containing Dnasupporting

confidence: 91%

“…To assess such changes in protein-DNA interactions, type II restriction endonucleases, in particular, that recognize and catalyze a double-strand DNA cleavage reaction at specific sequences have been used. DNA base substitutions within an endonuclease recognition site have been found to cause a wide range of effects on restriction enzymes, from complete inactivity to enhanced endonucleolytic cleavage of DNA, depending on the base analog substitution and restriction enzyme used (14,(18)(19)(20)(21)(22)(23).…”

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confidence: 99%

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Effects of 2-chloroadenine substitution in DNA on restriction endonuclease cleavage reactions

Hentosh

McCastlain

1991

Nucl Acids Res

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The purine analog, 2-chloro-2'-deoxyadenosine triphosphate (CldATP), was incorporated enzymatically in place of dATP into the minus strand of M13mp18 duplex DNA. Its effect on protein-DNA interactions was assessed by determining the amount of DNA cleavage by type II restriction endonucleases. Substitution of chloroadenine (CIAde) for adenine (Ade) in DNA appreciably decreased the amount and rate of DNA cleavage of the minus strand when the analog was situated within the appropriate endonuclease recognition site. CIAde residues flanking a restriction site had variable effects. SmaI cleaved both CIAde-containing and control substrates with equal efficiency. NarI, however, was stimulated 1.5-fold by the presence of CIAde outside its recognition site. The effects of analog incorporation on restriction enzyme cleavage of an opposing unsubstituted strand of duplex DNA was examined by enzymatically incorporating CIdATP into the complementary minus strand of a 36-base oligonucleotide. Endonucleolytic cleavage of both plus and minus strands was reduced on 36-mers containing CIAde residues located within only the minus strand. These data suggest that CIAde residues incorporated into a single DNA strand may have an appreciable effect on DNA-protein interactions that involve one or both strands of duplex DNA.

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Section: Results and Discussion Synthesis Of 'Clade'-containing Dnasupporting

confidence: 91%

mentioning

confidence: 99%

Effects of 2-chloroadenine substitution in DNA on restriction endonuclease cleavage reactions

Hentosh

McCastlain

1991

Nucl Acids Res

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“…In uninfected cells, the NM is thought to organize sites of cellular replication and transcription (9). The Ad genome has also been shown to localize to the NM through an interaction mediated by pTP (7,49). The studies reported here focused on understanding the mechanisms which influence the attachment of the pTP binding sites to the NM.…”

Section: Discussionmentioning

confidence: 99%

“…Ad DNA-binding protein stabilizes the single-stranded regions of the origin during synthesis. It has become clear that pTP mediates attachment of the Ad origin to specific sites on the nuclear matrix (NM) (7,49,60). Replication studies done by Fredman and colleagues (23,24) showed that pTP mutants (p233, p340, and p344) were wild type in in vitro replication assays but were defective for replication in vivo.…”

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confidence: 99%

Tyrosine kinase-dependent release of an adenovirus preterminal protein complex from the nuclear matrix

Angeletti

Engler

1996

J Virol

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Adenovirus (Ad) replicative complexes form at discrete sites on the nuclear matrix (NM) through the interaction of Ad preterminal protein (pTP). The NM is a highly salt-resistant fibrillar network which is known to anchor transcription, mRNA splicing, and DNA replication complexes. Incubation of rATP with NM to which pTP was bound caused the release of pTP as a pTP-NM complex with a size of 220 to 230 kDa; incubation with 5 adenylylimidodiphosphate (rAMP-PNP) showed no significant release, indicating that rATP hydrolysis was required. With NM extracts, it was shown that a pTP-NM complex which was capable of binding Ad origin DNA could be reconstituted in vitro. A number of high-molecular-weight NM proteins ranging in size from 120 to 200 kDa were identified on Far Western blots for their ability to bind pTP. rATP-dependent release of pTP from the NM was inhibited in a dose-dependent fashion by the addition of tyrosine kinase inhibitors, such as quercetin, methyl-2,5-dihydroxycinnamate, or genistein. NM-mediated phosphorylation of a poly(Glu, Tyr) substrate was also significantly abrogated by the addition of these compounds. rATP-dependent release of Ad DNA termini bound to the NM via pTP was also blocked by the addition of these inhibitors. These results indicate that a tyrosine kinase mechanism controls the release of pTP from its binding sites on the NM. These data support the concept that phosphorylation may play a key role in the modulation of pTP binding sites on the NM.

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“…Therefore, its replication proceeds via a protein-priming mechanism [192]. Cell fractionation studies indicated that adenovirus DNA is tightly bound to the nuclear matrix throughout the course of infection [193,194]. It has been shown that this attachment is mediated by the TP covalently bound to the DNA [195].…”

Section: Protein P1mentioning

confidence: 99%

Compartmentalization of prokaryotic DNA replication

2005

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It becomes now apparent that prokaryotic DNA replication takes place at specific intracellular locations. Early studies indicated that chromosomal DNA replication, as well as plasmid and viral DNA replication, occurs in close association with the bacterial membrane. Moreover, over the last several years, it has been shown that some replication proteins and specific DNA sequences are localized to particular subcellular regions in bacteria, supporting the existence of replication compartments. Although the mechanisms underlying compartmentalization of prokaryotic DNA replication are largely unknown, the docking of replication factors to large organizing structures may be important for the assembly of active replication complexes. In this article, we review the current state of this subject in two bacterial species, Escherichia coli and Bacillus subtilis, focusing our attention in both chromosomal and extrachromosomal DNA replication. A comparison with eukaryotic systems is also presented.

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The terminal regions of adenovirus and minute virus of mice DNAs are preferentially associated with the nuclear matrix in infected cells

Cited by 46 publications

References 69 publications

Effects of 2-chloroadenine substitution in DNA on restriction endonuclease cleavage reactions

Effects of 2-chloroadenine substitution in DNA on restriction endonuclease cleavage reactions

Tyrosine kinase-dependent release of an adenovirus preterminal protein complex from the nuclear matrix

Compartmentalization of prokaryotic DNA replication

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