Terminase
FunctionTerminase (Ter) is a key component of the DNA packaging machine found in bacteriophages and herpesviruses. The Ter complex is comprised of a small Ter subunit which is a recognition subunit and a large Ter subunit which is an endonuclease/translocase subunit [1]. The nuclease activity of the large Ter subunit is stimulated by ATP. The tripartite terminase complex of herpesvirus which contains 3 subunits (TRM1, TRM2 and TRM3), is found in the cytoplasm of infected cells and uses the cell's import machinery to enter the nucleus[2]. TRM3 has RNase H-like activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genome[3]. Structural highlightsThe large subunit of Ter is composed of an . ATP binds to the protein in a [4]. 3D Structures of terminase |
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ReferencesReferences
- ↑ PMID:22297528
- ↑ Sankhala RS, Lokareddy RK, Cingolani G. Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits. J Biol Chem. 2016 Mar 31. pii: jbc.M116.724393. PMID:27033706 doi:http://dx.doi.org/10.1074/jbc.M116.724393
- ↑ Heming JD, Huffman JB, Jones LM, Homa FL. Isolation and characterization of the herpes simplex virus 1 terminase complex. J Virol. 2014 Jan;88(1):225-36. doi: 10.1128/JVI.02632-13. Epub 2013 Oct 23. PMID:24155374 doi:http://dx.doi.org/10.1128/JVI.02632-13
- ↑ Zhao H, Christensen TE, Kamau YN, Tang L. Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage. Proc Natl Acad Sci U S A. 2013 May 14;110(20):8075-8080. Epub 2013 Apr 29. PMID:23630261 doi:10.1073/pnas.1301133110