Year: 2015
Type: review
Abstract: Translocation of viral double-stranded DNA (dsDNA) into the icosahedral prohead shell is catalyzed by TerL, a motor protein that has ATPase, endonuclease, and translocase activities. TerL, following endonucleolytic cleavage of immature viral DNA concatemer recognized by TerS, assembles into a pentameric ring motor on the prohead's portal vertex and uses ATP hydrolysis energy for DNA translocation. TerL's N-terminal ATPase is connected by a hinge to the C-terminal endonuclease. Inchworm models propose that modest domain motions accompanying ATP hydrolysis are amplified, through changes in electrostatic interactions, into larger movements of the C-terminal domain bound to DNA. In phage ϕ29, four of the five TerL subunits sequentially hydrolyze ATP, each powering translocation of 2.5 bp. After one viral genome is encapsidated, the internal pressure signals termination of packaging and ejection of the motor. Current focus is on the structures of packaging complexes and the dynamics of TerL during DNA packaging, endonuclease regulation, and motor mechanics.
Source: Annual Review of Virology
Authors: Venigalla B. Rao, Michael Feiss
Institutions: Catholic University of America, University of Iowa
Language: English
Subfield: Ecology
Field: Environmental Science
Domain: Physical Sciences
Open Access status: bronze
Awards: Mechanism of ATP-driven DNA Packaging in Bacteriophage T4, Structural studies of bacteriophage T4 and their potential medical applications, G2529869360, Structure and Function of Icosahedral Viruses, Mechanisms of Viral DNA Packaging: Biophysical, Biochemical, & Genetic Analysis, G3922485911, G4027423528, G44243821, Collaborative Research: Mechanisms of Termination of Viral DNA Packaging, Virus Chromosome Structure: Role in Development, Structural studies of bacteriophage T4 and their potential medical applications, G8434207751, G9000260610
OpenAlex ID: W1731131138