[Bacteriophage Mu transposase contains a fragment with primary structure similar to that of protein VPg covalently linked with poliovirus RNA].
A statistically valid similarity was found to exist between the amino acid sequences of poliovirus genome-linked protein VPg and a fragment of bacteriophage Mu transposase (Mu A protein). Based on this observation a hypothesis is proposed that the molecular mechanisms underlying the functions of the two proteins may be analogous. Both proteins are supposed to be site-specific endonucleases which form covalent linkage with the 5'-phosphate group of the nicked DNA or RNA strand. The amino acid residue participating in the formation of this linkage in MuA is tentatively identified as Tyr413.
Gorbalenia
A E
AE
Donchenko
A P
AP
Kunin
E V
EV
Blinov
V M
VM
D000595:Amino Acid Sequence; D003090:Coliphages / Q000201:enzymology / Q000235:genetics*; D009713:Nucleotidyltransferases / Q000235:genetics*; D017955:Poliovirus / Q000235:genetics* / Q000378:metabolism; D019895:Transposases; D014758:Viral Core Proteins; D014764:Viral Proteins / Q000235:genetics*
D014758:Viral Core Proteins; D014764:Viral Proteins; D009713:Nucleotidyltransferases; D019895:Transposases
Prisutstvie v transpozaze bakteriofaga Mu fragmenta, skhodnogo po pervichnoĭ strukture s belkom VPg, kovalentno sviazannykh s RNK poliovirusa.