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

Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation.

Microbiology (Reading, England) - 1 Dec 2003

Di Lallo G, Fagioli M, Barionovi D, Ghelardini P, Paolozzi L

Abstract excerpt

The ability of each of the nine Escherichia coli division proteins (FtsZ, FtsA, ZipA, FtsK, FtsQ, FtsL, FtsW, FtsI, FtsN) to interact with itself and with each of the remaining eight proteins was studied in 43 possible combinations of protein pairs by the two-hybrid system previously developed by the authors' group. Once the presumed interactions between the division proteins were determined, a model showing...

Read the complete abstract on PubMed

Topics

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

Share to Cell Division
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA, Bacterial

Share to Escherichia coli Proteins

Share to Macromolecular Substances

Share to Models, Biological

Share to Recombinant Proteins

Share to Two-Hybrid System Techniques

Source

Identifiers

PMID: 14663069
DOI: 10.1099/mic.0.26580-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation.PMID 14663069Read ↗

Essential and non-essential interactions in interactome networks: the Escherichia coli division proteins FtsQ-FtsN interaction.Semantic proximity Read ↗

Fluorescent assay for polymerization of purified bacterial FtsZ cell-division protein.Semantic proximity Read ↗

A 1 MDa protein complex containing critical components of the Escherichia coli divisome.Semantic proximity Read ↗

Interaction between two murein (peptidoglycan) synthases, PBP3 and PBP1B, in Escherichia coli.Semantic proximity Read ↗

Genetic analysis of the Escherichia coli FtsZ.ZipA interaction in the yeast two-hybrid system. Characterization of FtsZ residues essential for the interactions with ZipA and with FtsA.Semantic proximity Read ↗

Coordinated disassembly of the divisome complex in Escherichia coli.Semantic proximity Read ↗

Membrane topology of the N-terminus of the Escherichia coli FtsK division protein.Semantic proximity Read ↗

Domain-swapping analysis of FtsI, FtsL, and FtsQ, bitopic membrane proteins essential for cell division in Escherichia coli.Semantic proximity Read ↗

Phage-display and correlated mutations identify an essential region of subdomain 1C involved in homodimerization of Escherichia coli FtsA.Semantic proximity Read ↗

ZipA Uses a Two-Pronged FtsZ-Binding Mechanism Necessary for Cell Division.Semantic proximity Read ↗

DivIVA Regulates Its Expression and the Orientation of New Septum Growth in Deinococcus radiodurans.Semantic proximity Read ↗

Role of the C terminus of FtsK in Escherichia coli chromosome segregation.Semantic proximity Read ↗

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