FTSZ1-1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
FTSZ2-1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Co-localization
Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.
Publication
Distinct functions of chloroplast FtsZ1 and FtsZ2 in Z-ring structure and remodeling.
FtsZ, a cytoskeletal GTPase, forms a contractile ring for cell division in bacteria and chloroplast division in plants. Whereas bacterial Z rings are composed of a single FtsZ, those in chloroplasts contain two distinct FtsZ proteins, FtsZ1 and FtsZ2, whose functional relationship is poorly understood. We expressed fluorescently tagged FtsZ1 and FtsZ2 in fission yeast to investigate their intrinsic assembly ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
FTSZ2-1 FTSZ1-1 | FRET FRET An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins. | Low | - | BioGRID | - | |
FTSZ1-1 FTSZ2-1 | FRET FRET An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins. | Low | - | BioGRID | - | |
FTSZ1-1 FTSZ2-1 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - | |
FTSZ2-1 FTSZ1-1 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - | |
FTSZ1-1 FTSZ2-1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
FTSZ1-1 FTSZ2-1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
FTSZ2-1 FTSZ1-1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - |
Curated By
- BioGRID