Insight into DNA and Protein Transport in Double-Stranded DNA Viruses

The Structure of Bacteriophage N4

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

Research output: Contribution to journalArticle

55 Citations (Scopus)

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

Fingerprint

Bacteriophage N4
Viral Structures
DNA Viruses
Protein Transport
Virion
DNA
Genome
Cryoelectron Microscopy
Capsid
Capsid Proteins
DNA-Directed RNA Polymerases
Computational Biology
Proteins
Neck
Head
Viruses
Infection
brain synaptic membrane glycoprotein gp 50

Keywords

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

ASJC Scopus subject areas

  • Virology

Cite this

Insight into DNA and Protein Transport in Double-Stranded DNA Viruses : The Structure of Bacteriophage N4. / Choi, Kyung; McPartland, Jennifer; Kaganman, Irene; Bowman, Valorie D.; Rothman-Denes, Lucia B.; Rossmann, Michael G.

In: Journal of Molecular Biology, Vol. 378, No. 3, 02.05.2008, p. 726-736.

Research output: Contribution to journalArticle

Choi, Kyung ; McPartland, Jennifer ; Kaganman, Irene ; Bowman, Valorie D. ; Rothman-Denes, Lucia B. ; Rossmann, Michael G. / Insight into DNA and Protein Transport in Double-Stranded DNA Viruses : The Structure of Bacteriophage N4. In: Journal of Molecular Biology. 2008 ; Vol. 378, No. 3. pp. 726-736.
@article{84dfd74eed6947efadc2a7013f7f3f25,
title = "Insight into DNA and Protein Transport in Double-Stranded DNA Viruses: The Structure of Bacteriophage N4",
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.",
keywords = "bacteriophage N4, cryoelectron microscopy, DNA and protein transport, T = 9 quasi-symmetry, virion-encapsidated DNA-dependent RNA polymerase",
author = "Kyung Choi and Jennifer McPartland and Irene Kaganman and Bowman, {Valorie D.} and Rothman-Denes, {Lucia B.} and Rossmann, {Michael G.}",
year = "2008",
month = "5",
day = "2",
doi = "10.1016/j.jmb.2008.02.059",
language = "English (US)",
volume = "378",
pages = "726--736",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Insight into DNA and Protein Transport in Double-Stranded DNA Viruses

T2 - The Structure of Bacteriophage N4

AU - Choi, Kyung

AU - McPartland, Jennifer

AU - Kaganman, Irene

AU - Bowman, Valorie D.

AU - Rothman-Denes, Lucia B.

AU - Rossmann, Michael G.

PY - 2008/5/2

Y1 - 2008/5/2

N2 - 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.

AB - 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.

KW - bacteriophage N4

KW - cryoelectron microscopy

KW - DNA and protein transport

KW - T = 9 quasi-symmetry

KW - virion-encapsidated DNA-dependent RNA polymerase

UR - http://www.scopus.com/inward/record.url?scp=42249109989&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=42249109989&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2008.02.059

DO - 10.1016/j.jmb.2008.02.059

M3 - Article

VL - 378

SP - 726

EP - 736

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -