TY - JOUR
T1 - Insight into DNA and Protein Transport in Double-Stranded DNA Viruses
T2 - The Structure of Bacteriophage N4
AU - Choi, Kyung H.
AU - McPartland, Jennifer
AU - Kaganman, Irene
AU - Bowman, Valorie D.
AU - Rothman-Denes, Lucia B.
AU - Rossmann, Michael G.
N1 - Funding Information:
We thank Sheryl Kelly, Cheryl Towell, and Sharon Wilder for help in the preparation of the manuscript. We thank Marc Morais, Petr Leiman, Ye Xiang, Andrei Fokine, and Victor Kostyuchenko for helpful discussions; Noelia Salaberrios and Alexander Demidenko for the generation of N4 ORF 17am; and Abigail Markle for the purification of N4 phages. The work was supported by NSF grant MCB-0443899 (to M.G.R.) and NIH grant AI 12575 (to L.B.R.-D.).
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 - DNA and protein transport
KW - T = 9 quasi-symmetry
KW - bacteriophage N4
KW - cryoelectron microscopy
KW - virion-encapsidated DNA-dependent RNA polymerase
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U2 - 10.1016/j.jmb.2008.02.059
DO - 10.1016/j.jmb.2008.02.059
M3 - Article
C2 - 18374942
AN - SCOPUS:42249109989
SN - 0022-2836
VL - 378
SP - 726
EP - 736
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -