T4 phage gene uvsX product catalyzes homologous DNA pairing.

Yonesaki, Tetsuro; Minagawa, Teiichi

doi:10.1002/j.1460-2075.1985.tb04083.x

Cited by 105 publications

(52 citation statements)

References 41 publications

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“…It catalyzes the linear, duplex by single-strand circle strand-exchange reaction by pairing the 3'-homologous end of the linear duplex strand with the single-stranded circle followed by extension of the hybrid region toward the 5' end of the linear duplex strand (3'-to-5' direction) whereas all presently known eukaryotic proteins catalyze this reaction in the 5'-to-3' direction (22,23,(27)(28)(29)(30). Also, it requires a high protein/singlestranded DNA molar ratio approaching that required by the RecA and UvsX proteins, and the reaction shows a high degree of cooperativity (12,(15)(16)(17)(18)(19)(20)(21)(22).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Purification and characterization of an activity from Saccharomyces cerevisiae that catalyzes homologous pairing and strand exchange.

Kolodner¹,

Evans²,

Morrison³

1987

Proc. Natl. Acad. Sci. U.S.A.

123

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An activity that catalyzes the formation of joint molecules from linear M13mpl9 replicative form DNA and circular M13mpl9 viral DNA was purified 1000-to 2000-fold from mitotic Saccharomyces cerevisiae cells. The activity appeared to reside in a Mr 132,000 polypeptide. The reaction required that the substrates be homologous and also required Mg2'. There was no requirement for ATP. The reaction required stoichiometric amounts of protein and showed a cooperative dependence on protein concentration. Electron microscopic analysis of the joint molecules indicated they were formed by displacement of one strand of the linear duplex by the single-stranded circular molecule. This analysis also showed that heteroduplex formation started at the 3'-homologous end of the linear duplex strand followed by extension of the hybrid region toward the 5'-homologous end of the linear duplex strand (3'-to-5' direction).Genetic recombination is thought to occur by many different mechanisms (1-4). Common to the initiation of genetic recombination as postulated by many models is the pairing of DNA molecules at regions of homology followed by exchange of single strands to yield joint molecules containing regions of heteroduplex DNA (1-5). Strand exchange is probably the most extensively studied aspect of the enzymology of genetic recombination. Much of our knowledge comes from studies with the Escherichia coli RecA protein, which is required for genetic recombination, repair of DNA damage, and the SOS response (6-9). The RecA protein can catalyze the formation of a variety of joint DNA molecules (reviewed in refs, 9 and 10). Analysis of this process has shown it involves the pairing of a single-stranded DNA molecule with a homologous duplex DNA molecule (9,(11)(12)(13)(14)(15)

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Section: Discussionmentioning

confidence: 99%

“…Stable joint formation appears to initiate in both the 3'-to-5' and 5'-to-3' directions; however, extensive heteroduplex formation is polar and proceeds in the 3'-to-5' direction (22,23). The bacteriophage T4 UvsX protein appears to catalyze strandexchange reactions in a similar fashion to the RecA protein (24)(25)(26)(27),…”

mentioning

confidence: 99%

Purification and characterization of an activity from Saccharomyces cerevisiae that catalyzes homologous pairing and strand exchange.

Kolodner¹,

Evans²,

Morrison³

1987

Proc. Natl. Acad. Sci. U.S.A.

123

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show abstract

“…Both ADP-AlF 4 Ϫ and ATP-␥-S are being used in this case as analogs for ATP, but it can clearly be seen that the filament structure depends on which analog is being used. Numerous studies have shown that aluminum fluoride can serve as a very good non-hydrolyzable analog for ATP (28), whereas it has been shown that ATP-␥-S is slowly hydrolyzed by proteins such as RecA (29)(30)(31). The smaller pitch filaments, resembling the ''collapsed'' state of the RecA filament formed in the absence of ATP (25), have previously been seen with hRad51 protein on ssDNA when ATP-␥-S was used as a cofactor (23).…”

Section: N-terminal Domain Of Rad51mentioning

confidence: 99%

Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA

Xiong

Jacobs

West

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

226

247

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“…Proteins in this family include UvsX of a bacterial virus (Escherichia coli phage T4: ref. 16), RecA of various bacteria, RadA of archaea, and the Rad51-family proteins found in various eukaryotes from yeast to human beings (refs. 17 and 18, and see ref.…”

Section: Homologous Recombinationmentioning

confidence: 99%

Homologous genetic recombination as an intrinsic dynamic property of a DNA structure induced by RecA/Rad51-family proteins: A possible advantage of DNA over RNA as genomic material

Shibata

Nishinaka

Mikawa

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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Heteroduplex joints are general intermediates of homologous genetic recombination in DNA genomes. A heteroduplex joint is formed between a single-stranded region (or tail), derived from a cleaved parental double-stranded DNA, and homologous regions in another parental double-stranded DNA, in a reaction mediated by the RecA͞Rad51-family of proteins. In this reaction, a RecA͞ Rad51-family protein first forms a filamentous complex with the single-stranded DNA, and then interacts with the double-stranded DNA in a search for homology. Studies of the three-dimensional structures of single-stranded DNA bound either to Escherichia coli RecA or Saccharomyces cerevisiae Rad51 have revealed a novel extended DNA structure. This structure contains a hydrophobic interaction between the 2 methylene moiety of each deoxyribose and the aromatic ring of the following base, which allows bases to rotate horizontally through the interconversion of sugar puckers. This base rotation explains the mechanism of the homology search and base-pair switch between double-stranded and singlestranded DNA during the formation of heteroduplex joints. The pivotal role of the 2 methylene-base interaction in the heteroduplex joint formation is supported by comparing the recombination of RNA genomes with that of DNA genomes. Some simple organisms with DNA genomes induce homologous recombination when they encounter conditions that are unfavorable for their survival. The extended DNA structure confers a dynamic property on the otherwise chemically and genetically stable double-stranded DNA, enabling gene segment rearrangements without disturbing the coding frame (i.e., protein-segment shuffling). These properties may give an extensive evolutionary advantage to DNA.base-pair switch ͉ homologous pairing ͉ strand exchange ͉ NMR ͉ three-dimensional molecular structure DNA as a General Molecular Carrier of Genetic Information G enomic information generally is carried by double-stranded DNA. The double-stranded DNA structure discovered by Watson and Crick clearly explains the mechanisms of heredity, which include both the encoding of genetic information and its duplication as chemical properties of the molecule (1). In addition, the double-stranded structure enables cellular systems to recognize, as structural irregularities, erroneously incorporated nucleotides or lesions in bases, sugars, or the backbone strand, and to correct these errors by using the partner strand as a template. The genetic stability and the chemical inactivity of double-stranded DNA have been regarded as favorable molecular properties for its role as the carrier of genomic information. Evolution, which is a general attribute of the genome as well, has resulted in a variety of organisms, whose diversity arose not only as a result of changes in the genomic information, but also as a result of increased content and complexity. The faithful duplication and repair exhibited by the double-stranded DNA structure would seem to be incompatible with the process of evolution. Thus, evolution has b...

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T4 phage gene uvsX product catalyzes homologous DNA pairing.

Cited by 105 publications

References 41 publications

Purification and characterization of an activity from Saccharomyces cerevisiae that catalyzes homologous pairing and strand exchange.

Purification and characterization of an activity from Saccharomyces cerevisiae that catalyzes homologous pairing and strand exchange.

Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA

Homologous genetic recombination as an intrinsic dynamic property of a DNA structure induced by RecA/Rad51-family proteins: A possible advantage of DNA over RNA as genomic material

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