BAIT

MINE1

ARC12, ATMINE1, F23O10.25, F23O10_25, accumulation and replication of chloroplasts 12, homologue of bacterial MinE 1, AT1G69390
cell division topological specificity factor-like protein
GO Process (1)
GO Function (3)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

MIND

ACCUMULATION AND REPLICATION OF CHLOROPLASTS 11, ARC11, ATMIND1, MZF18.10, MZF18_10, AT5G24020
putative septum site-determining protein minD homolog
GO Process (1)
GO Function (4)
GO Component (3)
Arabidopsis thaliana (Columbia)

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.

Publication

The plastid division protein AtMinD1 is a Ca2+-ATPase stimulated by AtMinE1.

Aldridge C, Moller SG

Bacteria and plastids divide symmetrically through binary fission by accurately placing the division site at midpoint, a process initiated by FtsZ polymerization, which forms a Z-ring. In Escherichia coli precise Z-ring placement at midcell depends on controlled oscillatory behavior of MinD and MinE: In the presence of ATP MinD interacts with the FtsZ inhibitor MinC and migrates to the membrane ... [more]

J. Biol. Chem. Sep. 09, 2005; 280(36);31673-8 [Pubmed: 16014621]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
MIND MINE1
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
-
MIND MINE1
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
-
MINE1 MIND
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
-
MIND MINE1
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