Primary structure of the low molecular weight nucleic acid-binding proteins of murine leukemia viruses

• Published in: The Journal of biological chemistry 1981-08, Vol.256 (16), p.8400-8406
• Main Authors: Henderson, L E, Copeland, T D, Sowder, R C, Smythers, G W, Oroszlan, S
• Format: Article
• Language: English
• Subjects: AKR murine leukemia virus - analysis; Amino Acid Sequence; Friend murine leukemia virus - analysis; Gene Products, gag; Leukemia Virus, Murine - analysis; Moloney murine leukemia virus - analysis; Rauscher Virus - analysis; Species Specificity; Viral Proteins
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(19)68857-5

Murine leukemia viruses contain a low molecular weight basic protein, designated p10, which binds to single-stranded nucleic acids. The complete amino acid sequence of p10 from the Rauscher strain of virus has been determined. The partial amino acid sequences of p10s from Moloney, Friend, AKR, Gross, radiation leukemia, and BALB/2 viral strains have also been determined using microsequencing techniques. Rauscher p10 is composed of 56 amino acid residues; the other p10s are similar in size but differ from Rauscher by a few conservative amino acid substitutions. The structure of Rauscher p10 was compared to the structure of a functionally homologous protein from Rous avian sarcoma virus. The comparison revealed regions of amino acid sequence homologies which indicate a phylogenetic relationship between the murine and avian viral strains. The analyses revealed a periodic placement of three Cys residues and a Gly-His sequence. A structure involving these residues is found once in the murine protein and twice in the avian protein. A similar structure is seen in the single stranded nucleic acid binding protein of bacteriophage T4. However, in the latter case, the order of amino acid residues is inverted.