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 07:52, 18 August 2024
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