5cv3
C. remanei PGL-1 Dimerization Domain - Hg
Structural highlights
FunctionPGL1_CAERE Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate (PubMed:26787882). Essential role in male and female postembryonic germline development; maternally provided protein maintains a population of proliferating germ cells and zygotic expression is required for correct oogenesis (By similarity). Together with the P-granule component pgl-3, is involved in the formation of P-granules (By similarity). Together with pgl-3, probably recruits other granule components such as pos-1, mex-3 and glh-1 to P-granules (By similarity). In addition, may act redundantly with pgl-3 to protect germ cells from excessive germline apoptosis during normal oogenesis and development of the two gonadal arms (By similarity). This may in part be through regulating the localization of sir-2.1 which is involved in germ cell apoptosis (By similarity). May protect somatic cells from excessive apoptosis during normal development (By similarity).[UniProtKB:Q9TZQ3][1] Publication Abstract from PubMedCellular 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 alpha-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. PGL germ granule assembly protein is a base-specific, single-stranded RNase.,Aoki ST, Kershner AM, Bingman CA, Wickens M, Kimble J Proc Natl Acad Sci U S A. 2016 Jan 19. pii: 201524400. PMID:26787882[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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