Analysis of a mutation affecting the specificity domain for prohead binding of the bacteriophage lambda terminase.

Abstract:

:Genetic studies have identified a specificity domain for prohead binding in the C-terminal 32 amino acids of gpA, the large subunit of bacteriophage lambda terminase (S. Frackman, D. A. Siegele, and M. Feiss, J. Mol. Biol. 180:283-300, 1984). In the present work, an amber mutation, Aam42, in the fifth-to-last codon of the A gene was found to be lethal in nonsuppressing hosts. The mutation, expected to generate gpA lacking the last five amino acids, caused the production of a terminase that cut cos efficiently both in vivo and in vitro but was defective in DNA packaging. lambda Aam42 lysates contained unused proheads, consistent with a defect in prohead binding. Aam42 terminase was more strongly dependent than wild-type terminase on gpFI, the catalyst of prohead binding. Like wild-type terminase, Aam42 terminase did not cut cos in vivo when prohead assembly was blocked by a mutation in one of the genes encoding the prohead.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Sippy J,Feiss M

doi

10.1128/jb.174.3.850-856.1992

keywords:

subject

Has Abstract

pub_date

1992-02-01 00:00:00

pages

850-6

issue

3

eissn

0021-9193

issn

1098-5530

journal_volume

174

pub_type

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