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J Virol. 1980 October; 36(1): 115-119

Amino Acid Sequence Analysis of Reverse Transcriptase Subunits from Avian Myeloblastosis Virus

¹ Biological Carcinogenesis Program, Frederick Cancer Research Center, Frederick, Maryland 21701
² Saint Louis University Medical Center, Institute for Molecular Virology, St. Louis, Missouri 63110

ABSTRACT

The NH₂-terminal amino acid sequences of the and ß chains of avian myeloblastosis ß DNA polymerase were determined by using microsequence analysis in the subnanomole range and were found to be identical up to 17 residues. The common sequence was as follows: Thr-Val-Ala-Leu-His-Leu-Ala-Ile-Pro-Leu-Lys-Trp-Lys-Pro-Asn-His-Thr-. This result provides convincing chemical evidence that the chain is derived from the NH₂-terminal region of the ß chain by proteolytic cleavage, whereas the amino acid composition for these and ß subunits and p32 DNA endonuclease suggests that the latter is derived from the carboxyl-terminal region of the ß chain.

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