The L7Ae proteins mediate a widespread and highly functional protein–RNA interaction. (1st April 2019)

• Record Type: Journal Article
• Authors: Lilley, David M.J.
• Is Part Of: Biochemist. Volume 41:Number 2(2019)
• Page Start: 40
• Page End: 44
• Publication Date: 2019-04-01
• Subjects: Molecular biology -- Periodicals; Biochemistry -- Periodicals; 572
• DOI: 10.1042/BIO04102040
• Languages: English
• ISSNs: 0954-982X

Abstract

Abstract : The k-turn is a ubiquitous structural motif in RNA forming a very tight kink in the axis of helical RNA that plays an important role in many aspects of RNA function. L7Ae is a member of a superfamily of proteins that bind k-turns in RNA, stabilizing the tightly kinked conformation. They are extremely widespread and are important in the assembly of RNA–protein complexes central to translation, splicing and site-specific RNA modification. The interaction is exploited in order to regulate the synthesis of L7Ae proteins and is itself subject to regulation in box C/D snoRNP assembly by N6 methylation of a key adenine in the k-turn. Lastly, we can exploit the L7Ae–k-turn interaction in the construction of nanoscale assemblies.