Induction of structural changes in the bovine papillomavirus type 1 origin of replication by the viral E1 and E2 proteins
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Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteinsEffect of bovine papillomavirus E2 protein-specific monoclonal antibodies on papillomavirus DNA replication.Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex.Parvovirus initiator protein NS1 and RPA coordinate replication fork progression in a reconstituted DNA replication system.Characterization of the DNA-binding domain of the bovine papillomavirus replication initiator E1.The papillomavirus E1 protein forms a DNA-dependent hexameric complex with ATPase and DNA helicase activitiesIdentification of domains of the human papillomavirus type 11 E1 helicase involved in oligomerization and binding to the viral origin.Role of the ATP-binding domain of the human papillomavirus type 11 E1 helicase in E2-dependent binding to the originThe E1 initiator recognizes multiple overlapping sites in the papillomavirus origin of DNA replication.Episomal vectors for gene expression in mammalian cells.Sequential and ordered assembly of E1 initiator complexes on the papillomavirus origin of DNA replication generates progressive structural changes related to melting.E1 initiator DNA binding specificity is unmasked by selective inhibition of non-specific DNA binding.A multifunctional plasmid-encoded replication initiation protein both recruits and positions an active helicase at the replication origin.Initiation of DNA replication: lessons from viral initiator proteins.The bovine papillomavirus E2 protein modulates the assembly of but is not stably maintained in a replication-competent multimeric E1-replication origin complex.Mutational analysis of the 18-base-pair inverted repeat element at the bovine papillomavirus origin of replication: identification of critical sequences for E1 binding and in vivo replicationIsolation of an amino-terminal region of bovine papillomavirus type 1 E1 protein that retains origin binding and E2 interaction capacity.Functional interactions between papillomavirus E1 and E2 proteins.Bovine papillomavirus type 1 E1 and simian virus 40 large T antigen share regions of sequence similarity required for multiple functions.The initiator protein E1 binds to the bovine papillomavirus origin of replication as a trimeric ring-like structureCK2 phosphorylation inactivates DNA binding by the papillomavirus E1 and E2 proteins.The E1 proteins.Characterization of recombinant HPV6 and 11 E1 helicases: effect of ATP on the interaction of E1 with E2 and mapping of a minimal helicase domain.Role of ATP hydrolysis in the DNA translocase activity of the bovine papillomavirus (BPV-1) E1 helicase.Mechanism of DNA translocation in a replicative hexameric helicase.Identification of a short, hydrophilic amino acid sequence critical for origin recognition by the bovine papillomavirus E1 protein.Biochemical and electron microscopic image analysis of the hexameric E1 helicase.A fifteen-amino-acid peptide inhibits human papillomavirus E1-E2 interaction and human papillomavirus DNA replication in vitro.Distinct roles of two binding sites for the bovine papillomavirus (BPV) E2 transactivator on BPV DNA replication.Characterization of the minimal DNA binding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant proteinE1 recognition sequences in the bovine papillomavirus type 1 origin of DNA replication: interaction between half sites of the inverted repeats.Amino-terminal domains of the bovine papillomavirus type 1 E1 and E2 proteins participate in complex formation.Murine polyomavirus and simian virus 40 large T antigens produce different structural alterations in viral origin DNA.AP1 enhances polyomavirus DNA replication by promoting T-antigen-mediated unwinding of DNABinding of the E1 and E2 proteins to the origin of replication of bovine papillomavirus.Structure-based mutational analysis of the bovine papillomavirus E1 helicase domain identifies residues involved in the nonspecific DNA binding activity required for double trimer formation.Bending of adenovirus origin DNA by nuclear factor I as shown by scanning force microscopy is required for optimal DNA replicationHuman papillomavirus E2 down-regulates the human telomerase reverse transcriptase promoter.Co-operative interaction between the initiator E1 and the transcriptional activator E2 is required for replicator specific DNA replication of bovine papillomavirus in vivo and in vitro.The functions of human papillomavirus type 11 E1, E2, and E2C proteins in cell-free DNA replication.
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P2860
Induction of structural changes in the bovine papillomavirus type 1 origin of replication by the viral E1 and E2 proteins
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Induction of structural change ...... y the viral E1 and E2 proteins
@ast
Induction of structural change ...... y the viral E1 and E2 proteins
@en
type
label
Induction of structural change ...... y the viral E1 and E2 proteins
@ast
Induction of structural change ...... y the viral E1 and E2 proteins
@en
prefLabel
Induction of structural change ...... y the viral E1 and E2 proteins
@ast
Induction of structural change ...... y the viral E1 and E2 proteins
@en
P2093
P2860
P356
P1476
Induction of structural change ...... y the viral E1 and E2 proteins
@en
P2093
J A Borowiec
T G Gillette
P2860
P304
P356
10.1073/PNAS.91.19.8846
P407
P577
1994-09-01T00:00:00Z