The role of modifications in oligonucleotides in sequence recognition by <i>Mva</i>I restriction endonuclease

Кубарева, Е. А.; Pein, Claus‐Dietmar; Gromova, Elisaveta S.; Kuznezova, Svetlana A.; Tashlitzki, Vadim N.; Cech, Dieter; Shabarova, Zoe A.

doi:10.1111/j.1432-1033.1988.tb14236.x

Cited by 18 publications

(16 citation statements)

References 18 publications

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“…Polymer l a is cleaved by R -M u d as efficiently as DNA duplex 1. Substrate 4a is hydrolysed by R -M u d at a rate quite similar to DNA duplex 4 (Kubareva et al, 1988). These results rule out the possibility of a hydrophobic contact of R -M o d with the CH3 group of T (Fig.…”

Section: Possible Contacts In Complexes Of R -M U D and Recorii Withmentioning

confidence: 68%

Peculiarities of recognition of CC^A/_TGG sequences in DNA by restriction endonucleases MvaI and EcoRII

Gromova

Кубарева

Vinogradova

et al. 1991

J of Molecular Recognition

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To elucidate the mechanism of action of restriction endonucleases MvaI and EcoRII a study was made of their interaction with a set of synthetic substrates in which the heterocyclic bases or the sugar-phosphate backbone had been modified; individual nucleotide residues had been removed or replaced with hydrocarbon bridges, and mismatched base pairs had been introduced. The groups of atoms in the heterocyclic bases and the phosphates in the recognition site that produce the most significant influence on the functioning of endonucleases MvaI and EcoRII were discerned. Profound differences were found in the functioning of the MvaI and EcoRII neoschizomers. The catalytic activity of EcoRII is significantly affected by any alteration in the recognition site structure and conformation, with a modification in one strand of the substrate causing the same decrease in the hydrolysis rate of both strands. Endonuclease MvaI is tolerant to a number of structural abnormalities; the latter sometimes affect only hydrolysis of one strand of the recognition site. The enzyme can preferentially cleave one of the substrate strands. Mismatched base pairs retard and sometimes block the hydrolysis. The effect depends on the particular enzyme, mismatch and its location.

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Section: Possible Contacts In Complexes Of R -M U D and Recorii Withmentioning

confidence: 68%

Peculiarities of recognition of CC^A/_TGG sequences in DNA by restriction endonucleases MvaI and EcoRII

Gromova

Кубарева

Vinogradova

et al. 1991

J of Molecular Recognition

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“…The MvaI REase is accompanied by the cognate methyltransferase (MTase) which methylates the N4-amino group of the inner cytosine residue making the host DNA resistant to MvaI cleavage (6). The modification of the same cytosine to 5mC, which can be catalyzed by several physiologically unrelated MTases, is not protective against MvaI cleavage (7). …”

Section: Introductionmentioning

confidence: 99%

“…The enzyme completes the cleavage of substrates with a nick in one strand, irrespective of whether or not a phosphate is present at the nicking site (8). Moreover, selective modification of one DNA strand typically affects the cleavage of either the modified or the unmodified strand, depending on the nature of the modification, but only very drastic modifications impair cleavage of both strands (7,10). …”

Section: Introductionmentioning

confidence: 99%

Restriction endonuclease MvaI is a monomer that recognizes its target sequence asymmetrically

Kaus-Drobek¹,

Czapinska²,

Sokolowska³

et al. 2007

Nucleic Acids Research

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Restriction endonuclease MvaI recognizes the sequence CC/WGG (W stands for A or T, ‘/’ designates the cleavage site) and generates products with single nucleotide 5′-overhangs. The enzyme has been noted for its tolerance towards DNA modifications. Here, we report a biochemical characterization and crystal structures of MvaI in an apo-form and in a complex with target DNA at 1.5 Å resolution. Our results show that MvaI is a monomer and recognizes its pseudosymmetric target sequence asymmetrically. The enzyme consists of two lobes. The catalytic lobe anchors the active site residues Glu36, Asp50, Glu55 and Lys57 and contacts the bases from the minor grove side. The recognition lobe mediates all major grove interactions with the bases. The enzyme in the crystal is bound to the strand with T at the center of the recognition sequence. The crystal structure with calcium ions and DNA mimics the prereactive state. MvaI shows structural similarities to BcnI, which cleaves the related sequence CC/SGG and to MutH enzyme, which is a component of the DNA repair machinery, and nicks one DNA strand instead of making a double-strand break.

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“…The cognate DNA-methyltransferase M.MvaI modifies the internal cytosines to produce N4-methylcytosine: (C m4 CWGG/C m4 CWGG) (11). C5-methylation of the same cytosines does not protect against MvaI cleavage (12). MvaI was shown to recognize its pseudosymmetric target site as a monomer (13).…”

Section: Introductionmentioning

confidence: 99%

“…MvaI was shown to recognize its pseudosymmetric target site as a monomer (13). An interesting feature of the enzyme is its tolerance to a wide range of modifications within the recognition sequence (12). MvaI shares ∼20% sequence identity and structural similarity with BcnI, an REase recognizing the related pseudopalindromic sequence CC/SGG (S stands for G or C) (13–15).…”

Section: Introductionmentioning

confidence: 99%

The Type II restriction endonuclease MvaI has dual specificity

Stier

Kiss

2010

Nucleic Acids Research

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The MvaI restriction endonuclease cuts 5′-CC↓AGG-3′/5′-CC↑TGG-3′ sites as indicated by the arrows. N4-methylation of the inner cytosines (Cm4CAGG/Cm4CTGG) protects the site against MvaI cleavage. Here, we show that MvaI nicks the G-strand of the related sequence (CCGGG/CCCGG, BcnI site) if the inner cytosines are C5-methylated: Cm5C↓GGG/CCm5CGG. At M.SssI-methylated SmaI sites, where two oppositely oriented methylated BcnI sites partially overlap, double-nicking leads to double-strand cleavage (CCm5C↓GGG/CCm5C↑GGG) generating fragments with blunt ends. The double-strand cleavage rate and the stringency of substrate site recognition is lower at the methylation-dependent site than at the canonical target site. MvaI is the first restriction endonuclease shown to possess, besides the ‘normal’ activity on its unmethylated recognition site, also a methylation-directed activity on a different sequence.

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The role of modifications in oligonucleotides in sequence recognition by MvaI restriction endonuclease

Cited by 18 publications

References 18 publications

Peculiarities of recognition of CC^A/_TGG sequences in DNA by restriction endonucleases MvaI and EcoRII

Peculiarities of recognition of CC^A/_TGG sequences in DNA by restriction endonucleases MvaI and EcoRII

Restriction endonuclease MvaI is a monomer that recognizes its target sequence asymmetrically

The Type II restriction endonuclease MvaI has dual specificity

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The role of modifications in oligonucleotides in sequence recognition by MvaI restriction endonuclease

Cited by 18 publications

References 18 publications

Peculiarities of recognition of CCA/TGG sequences in DNA by restriction endonucleases MvaI and EcoRII

Peculiarities of recognition of CCA/TGG sequences in DNA by restriction endonucleases MvaI and EcoRII

Restriction endonuclease MvaI is a monomer that recognizes its target sequence asymmetrically

The Type II restriction endonuclease MvaI has dual specificity

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Peculiarities of recognition of CC^A/_TGG sequences in DNA by restriction endonucleases MvaI and EcoRII

Peculiarities of recognition of CC^A/_TGG sequences in DNA by restriction endonucleases MvaI and EcoRII