while the biologically relevant form of RT is the p66-p51 heterodimer, two recombinant homodimer forms of RT, p66-p66 and p51p51, are also catalytically active
1 * 66000 + 1 * 51000, the p66 subunit is composed of a DNA polymerase domain and an RNase H domain, whereas the p51 subunit contains only the polymerase domain
the two subunits are cloned and functionally expressed in Escherichia coli. The recombinant proteins are enzymatically active as homodimers, p66 and p51, as well as a heterodimer p66/p51. The p66/p51 heterodimer can perform strand displacement DNA synthesis of appriximately 300 bases. The homodimer p66 alone can carry out limited strand displacement DNA synthesis, but this activity is stimulated by the p51 subunit at a molar ratio of one molecule of p55 to five molecules of p51. The homodimer p51 itself is unable to fill a small gap of 26 nucleotides in a double-stranded DNA substrate and is not active by itself in strand displacement DNA synthesis
p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
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additional information
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
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two polypeptides of 66000 Da and 41000 Da are detectable in polymerase-expressing bacterial lysates. The 51000 Da protein appears to originate from the 66000 Da molecule
three polypeptides of 60000 Da, 68000 Da and 82000 Da are detected by SDS-PAGE. It seems likely that the 68000 Da and the 60000 Da polypeptide are degradation products of the 82000 Da polypeptide