Type III restriction endonucleases are heterotrimeric: comprising one helicase–nuclease subunit and a dimeric methyltransferase that binds only one specific DNA
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Title
Type III restriction endonucleases are heterotrimeric: comprising one helicase–nuclease subunit and a dimeric methyltransferase that binds only one specific DNA
Authors
Keywords
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Journal
NUCLEIC ACIDS RESEARCH
Volume 42, Issue 8, Pages 5139-5150
Publisher
Oxford University Press (OUP)
Online
2014-02-08
DOI
10.1093/nar/gku122
References
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Related references
Note: Only part of the references are listed.- Type III restriction-modification enzymes: a historical perspective
- (2013) Desirazu N. Rao et al. NUCLEIC ACIDS RESEARCH
- The Helicase-Like Domains of Type III Restriction Enzymes Trigger Long-Range Diffusion Along DNA
- (2013) F. W. Schwarz et al. SCIENCE
- Native ion mobility-mass spectrometry and related methods in structural biology
- (2012) A. Konijnenberg et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- DNA methyltransferases: Mechanistic models derived from kinetic analysis
- (2012) Ernst G. Malygin et al. CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
- Structure and operation of the DNA-translocating type I DNA restriction enzymes
- (2012) C. K. Kennaway et al. GENES & DEVELOPMENT
- Structural Insights into the Assembly and Shape of Type III Restriction–Modification (R–M) EcoP15I Complex by Small-Angle X-ray Scattering
- (2012) Yogesh K. Gupta et al. JOURNAL OF MOLECULAR BIOLOGY
- Do Charge State Signatures Guarantee Protein Conformations?
- (2012) Zoe Hall et al. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
- Native mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS
- (2011) Maria Chiara Monti et al. NUCLEIC ACIDS RESEARCH
- Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity
- (2011) Karol H. Wyszomirski et al. NUCLEIC ACIDS RESEARCH
- Maintaining a sense of direction during long-range communication on DNA
- (2010) Mark D. Szczelkun et al. BIOCHEMICAL SOCIETY TRANSACTIONS
- Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat
- (2010) K. van Aelst et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Dimeric/oligomeric DNA methyltransferases: an unfinished story
- (2009) Ernst G. Malygin et al. BIOLOGICAL CHEMISTRY
- Dimerization of DNA methyltransferase 1 is mediated by its regulatory domain
- (2009) Karin Fellinger et al. JOURNAL OF CELLULAR BIOCHEMISTRY
- S-Adenosyl homocysteine and DNA ends stimulate promiscuous nuclease activities in the Type III restriction endonuclease EcoPI
- (2009) L. J. Peakman et al. NUCLEIC ACIDS RESEARCH
- Type III restriction enzymes communicate in 1D without looping between their target sites
- (2009) Subramanian P. Ramanathan et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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