Search PubMedSearch

PubMed · 368561

A transducing lambda phage carrying grpE, a bacterial gene necessary for lambda DNA replication, and two ribosomal protein genes, rpsP (S16) and rplS (L19).

Abstract

A grpE mutation of Escherichia coli K12, which blocks DNA replication of the phage lambda (Saito and Uchida, 1977), was mapped at 56 min on the standard genetic map. A transducing lambda phage, lambdagrpE22, carrying the wild type allele of the grpE gene was constructed in vitro. Structures of lambdagrpE22 and its viable deletion derivatives were determined by electron microscopic analyses of appropriate heteroduplexes. Proteins coded by the bacterial DNA incorporated into the transducing phages were detected by two-dimensional gel electrophoresis. The results showed that the product of the grpE gene is a weakly acidic protein of molecular weight 24,000. Structural genes for two ribosomal proteins, rplS (L19) and rpsP (S16) were also shown to be carried by lambdagrpE22.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

H Saito, Y Nakamura, H Uchida. 1978-10-24. A transducing lambda phage carrying grpE, a bacterial gene necessary for lambda DNA replication, and two ribosomal protein genes, rpsP (S16) and rplS (L19).. https://doi.org/10.1007/bf00332523

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Bacteriophage fd gene II-protein. II. Specific cleavage and relaxation of supercoiled RF from filamentous phages.

Bacteriophage fd gene II-protein was characterized as an endonuclease which specifically nicked supercoiled replicative form (RF) of filamentous phages in the viral strand. No other supercoiled DNAs tested were attacked by the enzyme, nor were doubly closed fd RF in the relaxed state nor phage fd single strands. Maximal activity was found at pH 8.5 and 80 mM KCl using fd RFI of physiological superhelicity. Mg2+, but no other cofactor, was required for the cleavage reaction. A sealing activity was found to be associated with the enzyme. At a higher concentration of Mg2+ up to 40% of the reaction products were found as doubly closed relaxed fd RF. The protein was not found to be tightly attached to the cleaved strand.

Coliphages