How the BfiI restriction enzyme uses one active site to cut two DNA strands.
about
Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nucleaseExpression and purification of BmrI restriction endonuclease and its N-terminal cleavage domain variantsCatalytic domain of restriction endonuclease BmrI as a cleavage module for engineering endonucleases with novel substrate specificitiesRestriction endonuclease BpuJI specific for the 5'-CCCGT sequence is related to the archaeal Holliday junction resolvase familyOn the DNA cleavage mechanism of Type I restriction enzymesStructure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI.Protein assembly and DNA looping by the FokI restriction endonuclease.The other face of restriction: modification-dependent enzymesChemical display of pyrimidine bases flipped out by modification-dependent restriction endonucleases of MspJI and PvuRts1I familiesA genetic dissection of the LlaJI restriction cassette reveals insights on a novel bacteriophage resistance systemTemplate-directed addition of nucleosides to DNA by the BfiI restriction enzymeType II restriction endonucleases--a historical perspective and moreDNA synapsis through transient tetramerization triggers cleavage by Ecl18kI restriction enzyme.Natural and engineered nicking endonucleases--from cleavage mechanism to engineering of strand-specificityCharacterization of LlaKI, a New Metal Ion-Independent Restriction Endonuclease from Lactococcus lactis KLDS4.Site-specific DNA transesterification catalyzed by a restriction enzyme.The reaction mechanism of FokI excludes the possibility of targeting zinc finger nucleases to unique DNA sites.Mva1269I: a monomeric type IIS restriction endonuclease from Micrococcus varians with two EcoRI- and FokI-like catalytic domains.Sequence-specific DNA nicking endonucleases.CgII cleaves DNA using a mechanism distinct from other ATP-dependent restriction endonucleases.Target site cleavage by the monomeric restriction enzyme BcnI requires translocation to a random DNA sequence and a switch in enzyme orientation.A novel mechanism for the scission of double-stranded DNA: BfiI cuts both 3'-5' and 5'-3' strands by rotating a single active siteOne recognition sequence, seven restriction enzymes, five reaction mechanisms.The monomeric GIY-YIG homing endonuclease I-BmoI uses a molecular anchor and a flexible tether to sequentially nick DNA.Tetrameric restriction enzymes: expansion to the GIY-YIG nuclease family.Degenerate sequence recognition by the monomeric restriction enzyme: single mutation converts BcnI into a strand-specific nicking endonuclease.DNA looping by FokI: the impact of twisting and bending rigidity on protein-induced looping dynamics.Biochemical and mutagenic analysis of I-CreII reveals distinct but important roles for both the H-N-H and GIY-YIG motifsDiscovery of natural nicking endonucleases Nb.BsrDI and Nb.BtsI and engineering of top-strand nicking variants from BsrDI and BtsI.DNA cleavage by CgII and NgoAVII requires interaction between N- and R-proteins and extensive nucleotide hydrolysis.Transposition of the human Hsmar1 transposon: rate-limiting steps and the importance of the flanking TA dinucleotide in second strand cleavage.Targeting individual subunits of the FokI restriction endonuclease to specific DNA strands.UbaLAI is a monomeric Type IIE restriction enzyme.Homodimerisation-independent cleavage of dsRNA by a pestiviral nicking endoribonuclease.
P2860
Q24535057-E3F16D9F-91FE-452B-B17C-B7B326E81D71Q24649467-15B845C9-93BD-4A30-B762-83D3574AFACDQ24671370-98C99221-8CA3-44CC-A16F-7AE5B28E8F32Q24682734-71DEE559-7B05-45C2-8D3D-AF14194ADDA3Q24805170-23D1D7EF-E2D6-4595-B628-562A6E605F09Q24806247-2A23187E-8A60-42CA-9E25-0D8EAF6489FBQ25257871-AE359FDC-0CFD-467E-A5B9-0D8CE5BFBE38Q26851498-0E03F46D-C931-4FB3-8D8B-AC648F0A9BAAQ28542562-57B0130C-01A1-4E8A-9479-EF358BD39DFEQ33241520-059FE7D2-DCA0-467D-94FB-BD0033E59FEEQ33339247-8203AB23-8D1A-4B95-84FE-3B542937C02CQ33843093-0BFCDD1C-64CD-4207-894F-9EF2248BEE0EQ34298082-40BF5D4D-A922-43A6-8E85-F1949D559A05Q34474076-B5E4AF1C-8C13-4305-8041-91D25ECF0F56Q35361388-88C28F4A-C171-483C-9E19-0D2EA5864F6CQ35616738-C8DDC867-9468-4108-ABF9-92CFE1EFC26DQ37856408-6D007B20-F924-41DA-A51A-17BBF3F92EFAQ38319941-13F0804D-DBFF-415A-96FE-5B08F76684A2Q38583462-BECF2CA7-FD78-48EA-AFA7-F57E969E7CE3Q38601936-6D83443B-50ED-4B20-A063-E2BD29334722Q38855439-8754EB26-EC01-4D72-AE97-318A1C080895Q39986656-30EEB3AC-B1B8-47EF-B9E1-D792CBFC6952Q41023221-9AF568D4-CDAB-42B5-8A4F-7BBE16556772Q41074163-4A6038E1-F886-4390-A9F8-B438E7B2C840Q41820271-9278808C-93EB-4D53-A91A-843BFCAFB5E5Q42052209-024CB206-326D-4F5A-9802-FBB11BA6889CQ42052270-7727AC6D-544C-4F20-8405-0C3C2A8C2882Q42114363-53A36401-D59D-4880-B3A1-1CA2C0B35B22Q42413601-FD44B47E-040A-4EA2-81D1-50797F0A3B19Q42687145-C5BCAABD-B029-4781-B5FA-5AB5E1CCB9E7Q42944896-E015C92F-2C79-4C35-AAB8-E0538DC9E1C1Q43141069-39CFDD73-D1C7-4B88-843F-93FC7C825140Q47766790-06840633-25C5-4F76-B8E1-F40B045C88E9Q54940015-877522AE-1307-46C3-B6B5-F42036DCFC43
P2860
How the BfiI restriction enzyme uses one active site to cut two DNA strands.
description
2003 nî lūn-bûn
@nan
2003 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
How the BfiI restriction enzyme uses one active site to cut two DNA strands.
@ast
How the BfiI restriction enzyme uses one active site to cut two DNA strands.
@en
type
label
How the BfiI restriction enzyme uses one active site to cut two DNA strands.
@ast
How the BfiI restriction enzyme uses one active site to cut two DNA strands.
@en
prefLabel
How the BfiI restriction enzyme uses one active site to cut two DNA strands.
@ast
How the BfiI restriction enzyme uses one active site to cut two DNA strands.
@en
P2093
P2860
P356
P1476
How the BfiI restriction enzyme uses one active site to cut two DNA strands.
@en
P2093
Giedrius Sasnauskas
Stephen E Halford
Virginijus Siksnys
P2860
P304
P356
10.1073/PNAS.1131003100
P407
P577
2003-05-15T00:00:00Z