Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The in vivo function of phage phi29 nucleoid-associated protein p6 requires formation of dimers.

Gene - 21 Aug 2002

Abril Ana M, Salas Margarita, Hermoso José M

Abstract excerpt

The Bacillus subtilis phage phi29 nucleoid-associated protein p6 (103 amino acids) is essential for in vivo viral DNA replication and control of transcription, and it has been proposed to play a role in genome organization and compaction. This protein self-associates in vitro from preformed dimers forming high-molecular-weight oligomers and binds to double-stranded DNA giving rise to multimeric nucleoprotein...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacillus Phages
Share to Bacillus subtilis
Share to Dimerization

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA, Viral

Share to Genetic Complementation Test

Share to Temperature

Share to Viral Proteins

Share to Virus Replication

Source

Identifiers

PMID: 12383516
DOI: 10.1016/s0378-1119(02)00857-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The in vivo function of phage phi29 nucleoid-associated protein p6 requires formation of dimers.PMID 12383516Read ↗

Defining the structure-function relationships of bluetongue virus helicase protein VP6.Semantic proximity Read ↗

Isolation and analysis of mutants of double-stranded-RNA bacteriophage phi6 with altered packaging specificity.Semantic proximity Read ↗

Mutational analysis of the role of nucleoside triphosphatase P4 in the assembly of the RNA polymerase complex of bacteriophage phi6.Semantic proximity Read ↗

Novel dimeric structure of phage φ29-encoded protein p56: insights into uracil-DNA glycosylase inhibition.Semantic proximity Read ↗

Efficient DNA packaging of bacteriophage PRD1 requires the unique vertex protein P6.Semantic proximity Read ↗

Human DNA polymerase delta is a pentameric holoenzyme with a dimeric p12 subunitSemantic proximity Read ↗

Pleiotropic effect of protein P6 on the viral cycle of bacteriophage phi29.Semantic proximity Read ↗

Phage phi29 proteins p1 and p17 are required for efficient binding of architectural protein p6 to viral DNA in vivo.Semantic proximity Read ↗

Viral terminal protein directs early organization of phage DNA replication at the bacterial nucleoid.Semantic proximity Read ↗

Mutations within A 35 amino acid region of P6 influence self-association, inclusion body formation, and Caulimovirus infectivity.Semantic proximity Read ↗

Human DNA polymerase delta is a pentameric holoenzyme with dimeric p12 subunit: Implications in enzyme architecture and PCNA interactionSemantic proximity Read ↗

Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.