Insight into DNA and Protein Transport in Double-Stranded DNA Viruses: The Structure of Bacteriophage N4

Kyung H. Choi, Jennifer McPartland, Irene Kaganman, Valorie D. Bowman, Lucia B. Rothman-Denes, Michael G. Rossmann

Research output: Contribution to journalArticle

61 Scopus citations

Abstract

Bacteriophage N4 encapsidates a 3500-aa-long DNA-dependent RNA polymerase (vRNAP), which is injected into the host along with the N4 genome upon infection. The three-dimensional structures of wild-type and mutant N4 viruses lacking gp17, gp50, or gp65 were determined by cryoelectron microscopy. The virion has an icosahedral capsid with T = 9 quasi-symmetry that encapsidates well-organized double-stranded DNA and vRNAP. The tail, attached at a unique pentameric vertex of the head, consists of a neck, 12 appendages, and six ribbons that constitute a non-contractile sheath around a central tail tube. Comparison of wild-type and mutant virus structures in conjunction with bioinformatics established the identity and virion locations of the major capsid protein (gp56), a decorating protein (gp17), the vRNAP (gp50), the tail sheath (gp65), the appendages (gp66), and the portal protein (gp59). The N4 virion organization provides insight into its assembly and suggests a mechanism for genome and vRNAP transport strategies utilized by this unique system.

Original languageEnglish (US)
Pages (from-to)726-736
Number of pages11
JournalJournal of Molecular Biology
Volume378
Issue number3
DOIs
StatePublished - May 2 2008

Keywords

  • DNA and protein transport
  • T = 9 quasi-symmetry
  • bacteriophage N4
  • cryoelectron microscopy
  • virion-encapsidated DNA-dependent RNA polymerase

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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