Protein-nucleic acid interactions of LINE-1 ORF1p
| Autor: | Anthony V. Furano, M. Nabuan Naufer, Mark C. Williams |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
RNA-binding protein Article Open Reading Frames 03 medical and health sciences 0302 clinical medicine Animals Humans Binding site Ribonucleoprotein chemistry.chemical_classification Coiled coil Binding Sites biology DNA Cell Biology Amino acid Cell biology DNA-Binding Proteins Long interspersed nuclear element Kinetics Long Interspersed Nucleotide Elements 030104 developmental biology chemistry Chaperone (protein) biology.protein Nucleic acid 030217 neurology & neurosurgery Developmental Biology |
| Zdroj: | Seminars in cell & developmental biology |
| ISSN: | 1084-9521 |
| DOI: | 10.1016/j.semcdb.2018.03.019 |
| Popis: | Long interspersed nuclear element 1 (LINE-1 or L1) is the dominant retrotransposon in mammalian genomes. L1 encodes two proteins ORF1p and ORF2p that are required for retrotransposition. ORF2p functions as the replicase. ORF1p is a coiled coil-mediated trimeric, high affinity RNA binding protein that packages its full- length coding transcript into an ORF2p-containing ribonucleoprotein (RNP) complex, the retrotransposition intermediate. ORF1p also is a nucleic acid chaperone that presumably facilitates the proposed nucleic acid remodeling steps involved in retrotransposition. Although detailed mechanistic understanding of ORF1p function in this process is lacking, recent studies showed that the rate at which ORF1p can form stable nucleic acid-bound oligomers in vitro is positively correlated with formation of an active L1 RNP as assayed in vivo using a cell culture-based retrotransposition assay. This rate was sensitive to minor amino acid changes in the coiled coil domain, which had no effect on nucleic acid chaperone activity. Additional studies linking the complex nucleic acid binding properties to the conformational changes of the protein are needed to understand how ORF1p facilitates retrotransposition. |
| Databáze: | OpenAIRE |
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