Visualizing phosphodiester-bond hydrolysis by an endonuclease

Research output: Contribution to journalJournal articlepeer-review

Standard

Visualizing phosphodiester-bond hydrolysis by an endonuclease. / Molina, Rafael; Stella, Stefano; Redondo, Pilar; Gomez, Hansel; Marcaida, María José; Orozco, Modesto; Prieto, Jesús; Montoya, Guillermo.

In: Nature Structural and Molecular Biology, Vol. 22, No. 1, 01.2015, p. 65-72.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Molina, R, Stella, S, Redondo, P, Gomez, H, Marcaida, MJ, Orozco, M, Prieto, J & Montoya, G 2015, 'Visualizing phosphodiester-bond hydrolysis by an endonuclease', Nature Structural and Molecular Biology, vol. 22, no. 1, pp. 65-72. https://doi.org/10.1038/nsmb.2932

APA

Molina, R., Stella, S., Redondo, P., Gomez, H., Marcaida, M. J., Orozco, M., Prieto, J., & Montoya, G. (2015). Visualizing phosphodiester-bond hydrolysis by an endonuclease. Nature Structural and Molecular Biology, 22(1), 65-72. https://doi.org/10.1038/nsmb.2932

Vancouver

Molina R, Stella S, Redondo P, Gomez H, Marcaida MJ, Orozco M et al. Visualizing phosphodiester-bond hydrolysis by an endonuclease. Nature Structural and Molecular Biology. 2015 Jan;22(1):65-72. https://doi.org/10.1038/nsmb.2932

Author

Molina, Rafael ; Stella, Stefano ; Redondo, Pilar ; Gomez, Hansel ; Marcaida, María José ; Orozco, Modesto ; Prieto, Jesús ; Montoya, Guillermo. / Visualizing phosphodiester-bond hydrolysis by an endonuclease. In: Nature Structural and Molecular Biology. 2015 ; Vol. 22, No. 1. pp. 65-72.

Bibtex

@article{57b1e4536d394469acf4ad85df55b56a,
title = "Visualizing phosphodiester-bond hydrolysis by an endonuclease",
abstract = "The enzymatic hydrolysis of DNA phosphodiester bonds has been widely studied, but the chemical reaction has not yet been observed. Here we follow the generation of a DNA double-strand break (DSB) by the Desulfurococcus mobilis homing endonuclease I-DmoI, trapping sequential stages of a two-metal-ion cleavage mechanism. We captured intermediates of the different catalytic steps, and this allowed us to watch the reaction by 'freezing' multiple states. We observed the successive entry of two metals involved in the reaction and the arrival of a third cation in a central position of the active site. This third metal ion has a crucial role, triggering the consecutive hydrolysis of the targeted phosphodiester bonds in the DNA strands and leaving its position once the DSB is generated. The multiple structures show the orchestrated conformational changes in the protein residues, nucleotides and metals during catalysis.",
keywords = "DNA, Desulfurococcaceae, Endonucleases, Esters, Hydrolysis, Models, Molecular, Phosphates, Protein Conformation",
author = "Rafael Molina and Stefano Stella and Pilar Redondo and Hansel Gomez and Marcaida, {Mar{\'i}a Jos{\'e}} and Modesto Orozco and Jes{\'u}s Prieto and Guillermo Montoya",
year = "2015",
month = jan,
doi = "10.1038/nsmb.2932",
language = "English",
volume = "22",
pages = "65--72",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Visualizing phosphodiester-bond hydrolysis by an endonuclease

AU - Molina, Rafael

AU - Stella, Stefano

AU - Redondo, Pilar

AU - Gomez, Hansel

AU - Marcaida, María José

AU - Orozco, Modesto

AU - Prieto, Jesús

AU - Montoya, Guillermo

PY - 2015/1

Y1 - 2015/1

N2 - The enzymatic hydrolysis of DNA phosphodiester bonds has been widely studied, but the chemical reaction has not yet been observed. Here we follow the generation of a DNA double-strand break (DSB) by the Desulfurococcus mobilis homing endonuclease I-DmoI, trapping sequential stages of a two-metal-ion cleavage mechanism. We captured intermediates of the different catalytic steps, and this allowed us to watch the reaction by 'freezing' multiple states. We observed the successive entry of two metals involved in the reaction and the arrival of a third cation in a central position of the active site. This third metal ion has a crucial role, triggering the consecutive hydrolysis of the targeted phosphodiester bonds in the DNA strands and leaving its position once the DSB is generated. The multiple structures show the orchestrated conformational changes in the protein residues, nucleotides and metals during catalysis.

AB - The enzymatic hydrolysis of DNA phosphodiester bonds has been widely studied, but the chemical reaction has not yet been observed. Here we follow the generation of a DNA double-strand break (DSB) by the Desulfurococcus mobilis homing endonuclease I-DmoI, trapping sequential stages of a two-metal-ion cleavage mechanism. We captured intermediates of the different catalytic steps, and this allowed us to watch the reaction by 'freezing' multiple states. We observed the successive entry of two metals involved in the reaction and the arrival of a third cation in a central position of the active site. This third metal ion has a crucial role, triggering the consecutive hydrolysis of the targeted phosphodiester bonds in the DNA strands and leaving its position once the DSB is generated. The multiple structures show the orchestrated conformational changes in the protein residues, nucleotides and metals during catalysis.

KW - DNA

KW - Desulfurococcaceae

KW - Endonucleases

KW - Esters

KW - Hydrolysis

KW - Models, Molecular

KW - Phosphates

KW - Protein Conformation

U2 - 10.1038/nsmb.2932

DO - 10.1038/nsmb.2932

M3 - Journal article

C2 - 25486305

VL - 22

SP - 65

EP - 72

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 1

ER -

ID: 138737420