Terminase: Difference between revisions
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<StructureSection load='4ife' size='350' side='right' caption='Terminase large subunit complex with ATP (PDB code [[4ife]])' scene='77/775254/Cv/1'> | <StructureSection load='4ife' size='350' side='right' caption='Terminase large subunit complex with ATP (PDB code [[4ife]])' scene='77/775254/Cv/1'> | ||
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== Function == | == Function == | ||
'''Terminase''' (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 <ref>PMID:22'''297528</ref>. 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<ref>PMID:27033706</ref>. '''TRM3''' has RNase H-like activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genome<ref>PMID:24155374</ref>. | '''Terminase''' (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 <ref>PMID:22'''297528</ref>. 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<ref>PMID:27033706</ref>. '''TRM3''' has RNase H-like activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genome<ref>PMID:24155374</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
Latest revision as of 10:52, 18 August 2024
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