Structures of mammalian GLD-2 proteins reveal molecular basis of their functional diversity in mRNA and microRNA processing
| Autor: | Bing Yu, Jian-Xiong Feng, Li Luo, Xiao-Yan Ma, Song Gao, Jichang Wang, Hong Zhang, Jia-Li Hu, Shuang Liao, Yu-Lu Cao |
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| Rok vydání: | 2020 |
| Předmět: |
Cytoplasm
AcademicSubjects/SCI00010 RNA Stability Xenopus Proteins Biology Structural Biology RNA interference Genetics Animals RNA Messenger Caenorhabditis elegans Caenorhabditis elegans Proteins Polymerase Mammals Messenger RNA Oligonucleotide Polynucleotide Adenylyltransferase RNA Translation (biology) biology.organism_classification Nucleotidyltransferases Cell biology MicroRNAs Germ Cells biology.protein RNA Interference Poly A Function (biology) |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/gkaa578 |
| Popis: | The stability and processing of cellular RNA transcripts are efficiently controlled via non-templated addition of single or multiple nucleotides, which is catalyzed by various nucleotidyltransferases including poly(A) polymerases (PAPs). Germline development defective 2 (GLD-2) is among the first reported cytoplasmic non-canonical PAPs that promotes the translation of germline-specific mRNAs by extending their short poly(A) tails in metazoan, such as Caenorhabditis elegans and Xenopus. On the other hand, the function of mammalian GLD-2 seems more diverse, which includes monoadenylation of certain microRNAs. To understand the structural basis that underlies the difference between mammalian and non-mammalian GLD-2 proteins, we determine crystal structures of two rodent GLD-2s. Different from C. elegans GLD-2, mammalian GLD-2 is an intrinsically robust PAP with an extensively positively charged surface. Rodent and C. elegans GLD-2s have a topological difference in the β-sheet region of the central domain. Whereas C. elegans GLD-2 prefers adenosine-rich RNA substrates, mammalian GLD-2 can work on RNA oligos with various sequences. Coincident with its activity on microRNAs, mammalian GLD-2 structurally resembles the mRNA and miRNA processor terminal uridylyltransferase 7 (TUT7). Our study reveals how GLD-2 structurally evolves to a more versatile nucleotidyltransferase, and provides important clues in understanding its biological function in mammals. |
| Databáze: | OpenAIRE |
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