Binding properties of T4 gene 32 protein fragments carrying partially cleaved terminal domains

FEBS Letters

Casas-Finet, Jose R.¹ 

[1] Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510, USA

关键词: DNA-binding protein;    single-stranded;    Partial proteolysis;    Peptide mapping;    Equilibrium-binding isotherm;    ds;    double stranded;    g32P;    gene 32 product;    g32P-A;    g32P-B;    g32P-B′;    cleaved g32P lacking residues 254–301;    1–21 and 1–9;    respectively;    g32P-PR201 a frameshift mutant of g32P;    ss;    single stranded;   

DOI  :  10.1016/0014-5793(89)80666-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Analysis of fluorimetric equilibrium-binding isotherms of a proteolytic fragment of bacteriophage T4 gene 32 protein (g32P) lacking residues 1–9 shows that this region contains the site responsible for the function of the NH₂-terminal ‘B’ domain (residues 1–21). The end codon of the frameshift mutant g32P-PR201 has been identified as TAG at nucleotide position 852. The PR201 gene 32 product ends at Ser²⁸³ and carries a truncated COOH-terminal ‘A’ domain (residues 253–301). Fluorimetric titrations of g32P-PR201 with double-stranded DNA show that the functional residues of the A domain are located within the region spanning residues 284–301.

【 授权许可】

Unknown