FEBS Letters | |
Binding properties of T4 gene 32 protein fragments carrying partially cleaved terminal domains | |
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
【 预 览 】
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