7c36

Publication Abstract from PubMed

DNA binding proteins recognize DNA specifically or non-specifically using direct and indirect readout mechanisms like sliding, hopping, and diffusion. However, a common difficulty in explicitly elucidating any particular mechanism of site-specific DNA-protein recognition is the lack of knowledge regarding target sequences and inadequate account of non-specific interactions, in general. Here, we decipher the structural basis of target search performed by the key regulator of expression of c-myc proto-oncogene, the human RBMS1 protein. In this study, we have shown the structural reorganization of this multi-domain protein required for recognizing the specific c-myc promoter sequence. The results suggest that a synergy between structural re-organization and thermodynamics is necessary for the recognition of target sequences. The study presents another perspective of looking at the DNA-protein interactions.

Hinge like domain motion facilitates human RBMS1 protein binding to proto-oncogene c-myc promoter.,Aggarwal P, Bhavesh NS Nucleic Acids Res. 2021 Jun 4;49(10):5943-5955. doi: 10.1093/nar/gkab363. PMID:33999211^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.