Macrodomain Ter protein (MatP) (MatP)

Macrodomain Ter protein (MatP) is a specialized DNA-binding protein that organizes the terminus (Ter) region of the bacterial chromosome in species such as Escherichia coli (Mercier et al., 2008, PMC2583067). It functions by specifically recognizing and binding to 13-base pair DNA sequences known as matS sites, which are highly concentrated within the 800-kb Ter macrodomain. MatP coordinates the final stages of chromosome segregation with cytokinesis by forming a bridge to the cell division machinery; it interacts with the divisome protein ZapB, which in turn anchors the chromosomal Ter region to the midcell-localized FtsZ ring (Espeli et al., 2012, PubMed 22265405). Beyond its structural anchoring role, MatP acts as a molecular insulator that prevents the MukBEF condensin complex from compacting the Ter region prematurely, ensuring genomic stability (Nolivos et al., 2016, PMC4901358). Recent structural biology studies have also highlighted MatP's ability to form biomolecular condensates and interact with lipid membranes, suggesting its localization is regulated by multiple ligands including DNA and phospholipids (Valoti et al., 2024, bioRxiv; Monterroso et al., 2019, mBio). Although no clinical drugs currently target MatP, its essentiality for maintaining chromosome positioning and the absence of human homologs make it an attractive target for the development of novel, narrow-spectrum antibacterial agents.

Other names

DNA-binding protein MatPMacrodomain Ter-binding proteinmatS-binding protein

Inhibition of the specific binding between the MatP protein and matS DNA sequences, or disruption of the MatP-ZapB protein-protein interaction, which anchors the chromosomal terminus to the divisome machinery, leading to catastrophic defects in chromosome segregation and bacterial cell division.