Protein-protein interactions and glycerophospholipids in bromovirus and nodavirus RNA replication

作者: P. Ahlquist , S.-X. Wu , P. Kaesberg , C. C. Kao , R. Quadt

DOI: 10.1007/978-3-7091-9326-6_14

关键词:

摘要: The plant bromoviruses and animal nodaviruses are distinct groups of positive strand RNA viruses that have proven to be useful models for replication studies. Bromoviruses encode two large proteins required replication: 1a contains domains implicated in helicase capping functions, 2a a central polymerase-like domain. Using immunoprecipitation far-western blotting, we now shown la form specific complex vitro mapped the interacting domains. Molecular genetic data implicate 1a–2a suggest it supports coordinate action putative helicase, polymerase, locations implications evolution virus genomes bearing homologous genes fused vs. divided forms. For nodavirus Flock house (FHV), true replicase has been isolated carries out complete, highly active added FHV RNA, producing newly synthesized pre-dominantly ssRNA form. Positive synthesis this cell-free system is strongly dependent on addition any several glycerophospholipids. depends complete glycerophospholipid structure, including polar head group diacyl glycerol lipid portion, influenced by acyl chain length.

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