Directed evolution of restriction endonuclease BstYI to achieve increased substrate specificity

scientific article published in June 2002

Directed evolution of restriction endonuclease BstYI to achieve increased substrate specificity is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/S0022-2836(02)00343-1
P698PubMed publication ID12054862
P5875ResearchGate publication ID11318659

P2093author name stringJames C Samuelson
Shuang-yong Xu
P2860cites workStructure and function of type II restriction endonucleasesQ24555230
Understanding the immutability of restriction enzymes: crystal structure of BglII and its DNA substrate at 1.5 A resolutionQ27621185
Refinement of Eco RI endonuclease crystal structure: a revised protein chain tracingQ27685433
Structure of Bam HI endonuclease bound to DNA: partial folding and unfolding on DNA bindingQ27729783
Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysisQ27747308
Role of protein-induced bending in the specificity of DNA recognition: crystal structure of EcoRV endonuclease complexed with d(AAAGAT) + d(ATCTT)Q27749068
Recognition of flanking DNA sequences by EcoRV endonuclease involves alternative patterns of water-mediated contactsQ27765116
Randomization of genes by PCR mutagenesisQ33198019
How the EcoRI endonuclease recognizes and cleaves DNA.Q34541915
Generation of large libraries of random mutants in Bacillus subtilis by PCR-based plasmid multimerizationQ36877947
Saturation mutagenesis of His114 of EcoRI reveals relaxed-specificity mutantsQ38295212
Crosslinking the EcoRV restriction endonuclease across the DNA-binding site reveals transient intermediates and conformational changes of the enzyme during DNA binding and catalytic turnoverQ38331219
Changing the hydrogen-bonding potential in the DNA binding site of EcoRI by site-directed mutagenesis drastically reduces the enzymatic activity, not, however, the preference of this restriction endonuclease for cleavage within the site-GAATTC-.Q38344996
Inducible DNA repair systemsQ39826678
The 'endo-blue method' for direct cloning of restriction endonuclease genes in E. coli.Q40229405
Direct selection of binding proficient/catalytic deficient variants of BamHI endonucleaseQ40399034
Cloning and characterization of the Bg/II restriction-modification system reveals a possible evolutionary footprintQ42651983
Temperature-sensitive mutants of the EcoRI endonucleaseQ44548743
Mutational analysis of the function of Met137 and Ile197, two amino acids implicated in sequence-specific DNA recognition by the EcoRI endonuclease.Q52530957
Substrate recognition by the EcoRI endonuclease.Q54720062
Towards the design of rare cutting restriction endonucleases: using directed evolution to generate variants of EcoRV differing in their substrate specificity by two orders of magnitudeQ56902829
On the possibilities and limitations of rational protein design to expand the specificity of restriction enzymes: a case study employing EcoRV as the targetQ57267689
Protein engineering of the restriction endonuclease EcoRV . Structure-guided design of enzyme variants that recognize the base pairs flanking the recognition siteQ57267701
SOS induction as an in vivo assay of enzyme-DNA interactionsQ67996221
Effects of surrounding sequence on the suppression of nonsense codonsQ72695521
Genetic analysis of the base-specific contacts of BamHI restriction endonucleaseQ77901522
A mutant of BamHI restriction endonuclease which requires N6-methyladenine for cleavageQ77901524
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectdirected evolutionQ440681
P304page(s)673-683
P577publication date2002-06-01
P1433published inJournal of Molecular BiologyQ925779
P1476titleDirected evolution of restriction endonuclease BstYI to achieve increased substrate specificity
P478volume319

Reverse relations

cites work (P2860)
Q34482204A measure of the broad substrate specificity of enzymes based on 'duplicate' catalytic residues
Q28750208Alteration of Sequence Specificity of the Type IIS Restriction Endonuclease BtsI
Q24671370Catalytic domain of restriction endonuclease BmrI as a cleavage module for engineering endonucleases with novel substrate specificities
Q33585828Cloning of NruI and Sbo13I restriction and modification sstems in E. coli and amino acid sequence comparison of M.NruI and M.Sbo13I with other amino-methyltransferases
Q45996974Conformational transitions as determinants of specificity for the DNA methyltransferase EcoRI.
Q42859214Context dependence between subdomains in the DNA binding interface of the I-CreI homing endonuclease
Q35539178Crystallization and preliminary crystallographic analysis of the type IIL restriction enzyme MmeI in complex with DNA
Q25257169Engineering a rare-cutting restriction enzyme: genetic screening and selection of NotI variants
Q55359800Engineering altered protein-DNA recognition specificity.
Q44356433Engineering of restriction endonucleases: using methylation activity of the bifunctional endonuclease Eco57I to select the mutant with a novel sequence specificity
Q35207823Engineering proteins that bind, move, make and break DNA.
Q36802600Evolution of sequence specificity in a restriction endonuclease by a point mutation
Q24669929Generation of DNA cleavage specificities of type II restriction endonucleases by reassortment of target recognition domains
Q31091659In vitro selection of restriction endonucleases by in vitro compartmentalization
Q38353346Isolation of BsoBI restriction endonuclease variants with altered substrate specificity
Q33222949Laboratory-directed protein evolution
Q36909769Massively parallel characterization of restriction endonucleases
Q31120721Milestones in directed enzyme evolution.
Q27652792Molecular basis of xeroderma pigmentosum group C DNA recognition by engineered meganucleases
Q31155398Optimising enzyme function by directed evolution.
Q36497080Rational design of a chimeric endonuclease targeted to NotI recognition site
Q36280611Rational engineering of sequence specificity in R.MwoI restriction endonuclease
Q42072101Rational engineering of type II restriction endonuclease DNA binding and cleavage specificity
Q37991511Restriction endonucleases: natural and directed evolution
Q34323730Screening for catalytically active Type II restriction endonucleases using segregation-induced methylation deficiency
Q35991119Structure of Type IIL Restriction-Modification Enzyme MmeI in Complex with DNA Has Implications for Engineering New Specificities.

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