The L7Ae proteins mediate a widespread and highly functional protein-RNA interaction

TY - JOUR

T1 - The L7Ae proteins mediate a widespread and highly functional protein-RNA interaction

AU - Lilley, David M.J.

PY - 2019/4

Y1 - 2019/4

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/85075154432

U2 - 10.1042/bio04102040

DO - 10.1042/bio04102040

M3 - Article

AN - SCOPUS:85075154432

SN - 0954-982X

VL - 41

SP - 40

EP - 44

JO - Biochemist

JF - Biochemist

IS - 2

ER -