Thermostable Nucleoid Protein Cren7 Slides Along DNA and Rapidly Dissociates From DNA While Not Inhibiting the Sliding of Other DNA-binding Protein.

A nucleoid protein Cren7 compacts DNA, contributing to the living of Crenarchaeum in high temperature environment. In this study, we investigated the dynamic behavior of Cren7 on DNA and its functional relation using single-molecule fluorescence microscopy. We found two mobility modes of Cren7, sliding along DNA and pausing on it, and the rapid dissociation kinetics from DNA.

Molecular Analysis of Changes in DNA Binding Affinity and Bending Extent Induced by the Mutations on the Aromatic Amino Residues in Cren7.

Proteins from Crenarchaeal organisms exhibit remarkable thermal stability. The aromatic amino acids in Cren7, a Crenarchaeal protein, regulate protein stability and further modulate DNA binding and its compaction. Specific aromatic amino acids were mutated, and using spectroscopic and theoretical approaches, we have examined the effect of the mutation on the structure, DNA binding affinity, and DNA bending ability of Cren7.

Molecular contacts in the Cren7-DNA complex: A quantitative investigation for electrostatic interaction.

The molecular association of proteins with nucleic acids leading to the formation of macromolecular complexes is a crucial step in several biological processes. Stabilization of these complexes involves electrostatic interactions between ion pairs (salt bridges) of nucleic acid phosphates and protein side chains. The crenarchaeal DNA binding protein, Cren7 plays a key role in the regulation of chromosomal structure and gene expression in eukaryotic extremophiles.

Structural and thermodynamic insights into the Cren7 mediated DNA organization in Crenarchaeota.

Archaea have histone homologues and chromatin proteins to organize their DNA into a compact form. This allows them to survive in extreme climates. Cren7 is one such chromatin protein conserved in Crenarchaeota.

Critical insights into the interactions of heat shock protein 70 with phospholipids.

Heat shock proteins (Hsps) stabilize the newly synthesized polypeptide chains preventing them from aggregation. They contribute to systemic response under stress and thus behave as signaling molecules. Hsp70 has been detected on the surface of stressed cells.