Binding and folding in transcriptional complexes. (February 2021)

• Record Type: Journal Article
• Authors: Smith, Ngaio C; Kuravsky, Mikhail; Shammas, Sarah L; Matthews, Jacqueline M
• Is Part Of: Current opinion in structural biology. Volume 66(2021)
• Page Start: 156
• Page End: 162
• Publication Date: 2021-02
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2020.10.026
• Languages: English
• ISSNs: 0959-440X

Abstract

Graphical abstract: Highlights: Many aspects of transcription factor function involve folding upon binding. Intrinsic disorder plays a role in both DNA binding and transcriptional activation. Technological advances allow closer investigation into mechanisms of binding and folding. Binding does not necessarily promote folding, rather complexes exist on a spectrum from highly disordered to highly ordered. Electrostatics and heterogeneity play important roles binding and folding. Abstract : Transcription factors are among the classes of proteins with the highest levels of disorder. Investigation of these regulatory proteins is uncovering not just the mechanisms that underlie gene regulation, but relationships that apply to all intrinsically disordered proteins. Recent studies confirm that binding does not necessarily induce folding but that when it does, it tends to follow induced fit mechanisms. Other work emphasises the importance of electrostatics to interactions involving intrinsically disordered proteins, and roles of intrinsic disorder in phase transitions. All these features help direct transcription factors to target sites in the genome to upregulate or downregulate transcription.