The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes.

Escherichia coli DiaA is a DnaA-binding protein that is required for the timely initiation of chromosomal replication during the cell cycle. In this study, we determined the crystal structure of DiaA at 1.8 A resolution.

Motion-JPEG2000 codec compensated for interlaced scanning videos.

This paper presents an implementation scheme of Motion-JPEG2000 (MJP2) integrated with invertible deinterlacing. In previous work, we developed an invertible deinterlacing technique that suppresses the comb-tooth artifacts which are caused by field interleaving for interlaced scanning videos, and affect the quality of scalable frame-based codecs, such as MJP2. Our technique has two features, where sampling density is preserved and image quality is recovered by an inverse process.

Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.

In Escherichia coli, the activity of ATP-bound DnaA protein in initiating chromosomal replication is negatively controlled in a replication-coordinated manner. The RIDA (regulatory inactivation of DnaA) system promotes DnaA-ATP hydrolysis to produce the inactivated form DnaA-ADP in a manner depending on the Hda protein and the DNA-loaded form of the beta-sliding clamp, a subunit of the replicase holoenzyme. A highly functional form of Hda was purified and shown to form a homodimer in solution, and two Hda dimers were found to associate with a single clamp molecule.

DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication.

The DnaA protein is the initiator of Escherichia coli chromosomal replication. In this study, we identify a novel DnaA-associating protein, DiaA, that is required for the timely initiation of replication during the cell cycle. DiaA promotes the growth of specific temperature-sensitive dnaA mutants and ensures stable minichromosome maintenance, whereas DiaA does not decrease the cellular DnaA content.