7lj3 | pdb_00007lj3
Structure of human transfer RNA visualized in the cytomegalovirus, a DNA virus
Structural highlights
FunctionPP150_HCMVA Participates in the last steps of viral maturation and release. Associates with nuclear capsids prior to DNA encapsidation and later preserves the integrity of nucleocapsids through secondary envelopment at the assembly compartment. Interacts with host CCNA2 and thereby blocks the onset of lytic gene expression to promote establishment of a quiescent state of infection in undifferentiated cells.[1] [2] [3] [4] [5] Publication Abstract from PubMedUnder the Baltimore nucleic acid-based virus classification scheme, the herpesvirus human cytomegalovirus (HCMV) is a Class I virus, meaning that it contains a double-stranded DNA genome-and no RNA. Here, we report sub-particle cryoEM reconstructions of HCMV virions at 2.9 A resolution revealing structures resembling non-coding transfer RNAs (tRNAs) associated with the virion's capsid-bound tegument protein, pp150. Through deep sequencing, we show that these RNA sequences match human tRNAs, and we built atomic models using the most abundant tRNA species. Based on our models, tRNA recruitment is mediated by the electrostatic interactions between tRNA phosphate groups and the helix-loop-helix motif of HCMV pp150. The specificity of these interactions may explain the absence of such tRNA densities in murine cytomegalovirus and other human herpesviruses. Structure of human cytomegalovirus virion reveals host tRNA binding to capsid-associated tegument protein pp150.,Liu YT, Strugatsky D, Liu W, Zhou ZH Nat Commun. 2021 Sep 17;12(1):5513. doi: 10.1038/s41467-021-25791-1. PMID:34535641[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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