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FEBS Lett. 1989 Jun 5;249(2):396-400.

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

Author information

1
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510.

Abstract

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.

PMID:
2786820
DOI:
10.1016/0014-5793(89)80666-0
[Indexed for MEDLINE]
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