PGL germ granule assembly protein is a base-specific, single-stranded RNase

Proceedings of the National Academy of Sciences of the United States of America
Scott T AokiJudith Kimble

Abstract

Cellular RNA-protein (RNP) granules are ubiquitous and have fundamental roles in biology and RNA metabolism, but the molecular basis of their structure, assembly, and function is poorly understood. Using nematode "P-granules" as a paradigm, we focus on the PGL granule scaffold protein to gain molecular insights into RNP granule structure and assembly. We first identify a PGL dimerization domain (DD) and determine its crystal structure. PGL-1 DD has a novel 13 α-helix fold that creates a positively charged channel as a homodimer. We investigate its capacity to bind RNA and discover unexpectedly that PGL-1 DD is a guanosine-specific, single-stranded endonuclease. Discovery of the PGL homodimer, together with previous results, suggests a model in which the PGL DD dimer forms a fundamental building block for P-granule assembly. Discovery of the PGL RNase activity expands the role of RNP granule assembly proteins to include enzymatic activity in addition to their job as structural scaffolds.

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Citations

Jan 5, 2019·Physical Review Letters·Louise M JawerthElisabeth Fischer-Friedrich
Feb 9, 2021·Wiley Interdisciplinary Reviews. RNA·Nivedita Mukherjee, Chandrama Mukherjee
Feb 14, 2021·Nature Communications·Scott Takeo AokiJudith Kimble
Nov 14, 2021·RNA·John Paul Tsu Ouyang, Geraldine Seydoux

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