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Murine leukemia virus protease is encoded by the gag-pol gene and is synthesized through suppression of an amber termination codon.
Open accessAbstract
We have purified from Moloney murine leukemia virus (Mo-MuLV) a protease that has the capacity of accurately cleaving the polyprotein precursor Pr65gag into the mature viral structural proteins. Both the NH2- and COOH-terminal amino acid sequences have been determined and aligned with the amino acid sequence deduced from the DNA sequence of Mo-MuLV by other workers. The results show that: (i) the protease is located at the 5' end of the pol gene, and the first four amino acids are overlapped with the 3' end of the gag gene; (ii) the fifth amino acid residue is glutamine, which is inserted by suppression of the UAG termination codon at the gag-pol junction; and (iii) the protease is composed of 125 amino acids with calculated Mr = 13,315, and the COOH terminus of the protease is adjacent to the NH2 terminus of reverse transcriptase. The map order of the gag-pol gene is proposed to be 5'-p15-p12-p30-p10-protease-reverse transcriptase-endonuclease-3'.
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“…of translational readthrough involves suppressing the termination codon at the end of the gag gene, thereby maintaining the same reading frame during the translation of Gag and Pol, as has been observed in MLV (Yoshinaka et al. 1985a , ten Dam et al. 1990 , Wills et al. 1991 , Goff 2004 ).”
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Metadata
- Authors
- Yoshinaka, Y., Katoh, I., Copeland, T. D., & Oroszlan, S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1985-03
- Volume
- 82
- Issue
- 6
- Pages
- 1618-1622
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2008826548
- Cited by
- 335
- References
- 0
- FWCI
- 13.36
- Type
- journal article
- Language
- en
- Open access
- green
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