Ozaki et al., 2012 - Google Patents
Differentiation of the DnaA-oriC subcomplex for DNA unwinding in a replication initiation complexOzaki et al., 2012
View HTML- Document ID
- 10143467838488810734
- Author
- Ozaki S
- Noguchi Y
- Hayashi Y
- Miyazaki E
- Katayama T
- Publication year
- Publication venue
- Journal of Biological Chemistry
External Links
Snippet
In Escherichia coli, ATP-DnaA multimers formed on the replication origin oriC promote duplex unwinding, which leads to helicase loading. Based on a detailed functional analysis of the oriC sequence motifs, we previously proposed that the left half of oriC forms an ATP …
- 230000000977 initiatory 0 title description 89
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6813—Hybridisation assays
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2310/00—Structure or type of the nucleic acid
- C12N2310/10—Type of nucleic acid
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N27/00—Investigating or analysing materials by the use of electric, electro-chemical, or magnetic means
- G01N27/26—Investigating or analysing materials by the use of electric, electro-chemical, or magnetic means by investigating electrochemical variables; by using electrolysis or electrophoresis
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Ozaki et al. | Differentiation of the DnaA-oriC subcomplex for DNA unwinding in a replication initiation complex | |
| Ozaki et al. | A common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication origin | |
| Keyamura et al. | DiaA dynamics are coupled with changes in initial origin complexes leading to helicase loading | |
| Su'etsugu et al. | Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex | |
| Kawakami et al. | Formation of an ATP-DnaA-specific initiation complex requires DnaA Arginine 285, a conserved motif in the AAA+ protein family | |
| Wu et al. | Calmodulin kinase II attenuation of gene transcription by preventing cAMP response element-binding protein (CREB) dimerization and binding of the CREB-binding protein | |
| Edwards et al. | Mcm2–7 complexes bind chromatin in a distributed pattern surrounding the origin recognition complex inxenopus egg extracts | |
| Lee et al. | Ataxia telangiectasia-mutated (ATM) kinase activity is regulated by ATP-driven conformational changes in the Mre11/Rad50/Nbs1 (MRN) complex | |
| Noble et al. | The Dbp5 cycle at the nuclear pore complex during mRNA export II: nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1 | |
| Liou et al. | DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E | |
| Lusetti et al. | The DinI protein stabilizes RecA protein filaments | |
| Tackett et al. | Multiple full-length NS3 molecules are required for optimal unwinding of oligonucleotide DNA in vitro | |
| Li et al. | The DrrAB efflux system of Streptomyces peucetius is a multidrug transporter of broad substrate specificity | |
| Kozlov et al. | Regulation of single-stranded DNA binding by the C termini of Escherichia coli single-stranded DNA-binding (SSB) protein | |
| Noguchi et al. | The Arg fingers of key DnaA protomers are oriented inward within the replication origin oriC and stimulate DnaA subcomplexes in the initiation complex | |
| Bussen et al. | Holliday junction processing activity of the BLM-Topo IIIα-BLAP75 complex | |
| Byrd et al. | Pif1 helicase unfolding of G-quadruplex DNA is highly dependent on sequence and reaction conditions | |
| Melton et al. | Combinatorial control of signal-induced exon repression by hnRNP L and PSF | |
| Phelan et al. | Distinct HOX N-terminal arm residues are responsible for specificity of DNA recognition by HOX monomers and HOX· PBX heterodimers | |
| Dou et al. | The DNA binding properties of the Escherichia coli RecQ helicase | |
| Kasho et al. | Cooperative DnaA binding to the negatively supercoiled datA locus stimulates DnaA-ATP hydrolysis | |
| Liu et al. | The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding | |
| Choudhary et al. | Biochemical and kinetic characterization of the DNA helicase and exonuclease activities of Werner syndrome protein | |
| Charenton et al. | mRNA decapping: finding the right structures | |
| Tanaka et al. | Stabilization of a stalled replication fork by concerted actions of two helicases |