Role of the N-terminal domain of phi C31 integrase in attB-attP synapsis

Paul A. Rowley; Margaret C. M. Smith

doi:10.1128/JB.00612-08

Role of the N-terminal domain of phi C31 integrase in attB-attP synapsis

Paul A. Rowley, Margaret C. M. Smith

Medical Sciences

Inst Med Sci

Research output: Contribution to journal › Article › peer-review

20 Citations (Scopus)

Abstract

phi C31 integrase is a serine recombinase containing an N-terminal domain (NTD) that provides catalytic activity and a large C-terminal domain that controls which pair of DNA substrates is able to synapse. We show here that substitutions in amino acid V129 in the NTD can lead to defects in synapsis and DNA cleavage, indicating that the NTD also has an important role in synapsis.

Original language	English
Pages (from-to)	6918-6921
Number of pages	4
Journal	Journal of Bacteriology
Volume	190
Issue number	20
Early online date	8 Aug 2008
DOIs	https://doi.org/10.1128/JB.00612-08
Publication status	Published - Oct 2008

Keywords

site-specific recombination
BXB1 integration
DNA cleavage
resolvase
directionality

Access to Document

10.1128/JB.00612-08

Cite this

@article{e9164dfbf6684709bf916dab826be433,

title = "Role of the N-terminal domain of phi C31 integrase in attB-attP synapsis",

abstract = "phi C31 integrase is a serine recombinase containing an N-terminal domain (NTD) that provides catalytic activity and a large C-terminal domain that controls which pair of DNA substrates is able to synapse. We show here that substitutions in amino acid V129 in the NTD can lead to defects in synapsis and DNA cleavage, indicating that the NTD also has an important role in synapsis.",

keywords = "site-specific recombination, BXB1 integration, DNA cleavage, resolvase, directionality",

author = "Rowley, {Paul A.} and Smith, {Margaret C. M.}",

year = "2008",

month = oct,

doi = "10.1128/JB.00612-08",

language = "English",

volume = "190",

pages = "6918--6921",

journal = "Journal of Bacteriology",

issn = "0021-9193",

publisher = "American Society for Microbiology",

number = "20",

}

TY - JOUR

T1 - Role of the N-terminal domain of phi C31 integrase in attB-attP synapsis

AU - Rowley, Paul A.

AU - Smith, Margaret C. M.

PY - 2008/10

Y1 - 2008/10

N2 - phi C31 integrase is a serine recombinase containing an N-terminal domain (NTD) that provides catalytic activity and a large C-terminal domain that controls which pair of DNA substrates is able to synapse. We show here that substitutions in amino acid V129 in the NTD can lead to defects in synapsis and DNA cleavage, indicating that the NTD also has an important role in synapsis.

AB - phi C31 integrase is a serine recombinase containing an N-terminal domain (NTD) that provides catalytic activity and a large C-terminal domain that controls which pair of DNA substrates is able to synapse. We show here that substitutions in amino acid V129 in the NTD can lead to defects in synapsis and DNA cleavage, indicating that the NTD also has an important role in synapsis.

KW - site-specific recombination

KW - BXB1 integration

KW - DNA cleavage

KW - resolvase

KW - directionality

U2 - 10.1128/JB.00612-08

DO - 10.1128/JB.00612-08

M3 - Article

SN - 0021-9193

VL - 190

SP - 6918

EP - 6921

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 20

ER -

Role of the N-terminal domain of phi C31 integrase in attB-attP synapsis

Abstract

Keywords

Access to Document

Fingerprint

Cite this