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Biomedical subjects

N D Zinder

Publications and source records attributed to N D Zinder.

At least 37 records · Page 2Linked to original sources
PubMed1983

The morphogenetic signal of bacteriophage f1.

The genome of the single-stranded DNA phage f1 contains an intergenic region (IG), 508-nucleotides long, that does not code for any known protein. By use of a system of chimeric plasmids haboring different f1 fragments, we had previously shown that this region contains, in addition to the f1 'functional origin' of DNA replication, a signal of less than 300 nucleotides required for efficient morphogenesis to occur ('morphogenetic signal'). In the present study, we have localized this signal to within a sequence of less that 60 nucleotides of almost perfect palindromic symmetry at the genet IV/IG border. We also present data indicating that the morphogenetic signal is not necessary for the synthesis of single-stranded DNA, but is necessary only at some later step during virion maturation.

Base Sequence↗
PubMed1982

Effects of bacteriophage f1 gene III protein on the host cell membrane.

Plasmids which encode bacteriophage f1 coat protein genes VIII and III are responsible for a number of unusual properties suggesting that they have a drastic effect on the bacterial outer membrane. Analysis of several such recombinant plasmids and selection of mutant plasmids unable to cause this effect established that the properties were caused by gene III protein or its amino-terminal fragment.

Amino Acid Sequence↗
PubMed1982

Initiation and termination of phage f1 plus-strand synthesis.

The origin of DNA replication of bacteriophage f1 contains a nucleotide sequence that is used both for the initiation of viral (plus) strand synthesis and for its termination. With chimeric plasmids containing two f1 functional origins in the same orientation, synthesis of chimeric plus-strand DNA is initiated, after f1 infection, at either one of the two f1 origins and is terminated at the other. Thus, the chimeric plasmids segregate into two replicons, each of them containing only one f1 origin. This system has been used to test several fragments of the f1 origin varying in size or in nucleotide sequence for their ability to function in either initiation or termination of viral strand synthesis. Our data show that the f1 origin is composed of two overlapping but distinct domains (signals), one for initiation and the other for termination of plus-strand synthesis.

Base Sequence↗
PubMed1982

Another gene affecting sexual expression of Escherichia coli.

We have examined the relationship between two chromosomal mutations of Escherichia coli K-12, fexA (0 min) and fexB (85 min), in regulating expression of the F sex factor. Together, fexA and fexB exert a pleiotropic effect on the expression of the F tra genes. F pilus synthesis, conjugal donor activity, and surface exclusion activity are all inhibited in the fexA fexB mutant. Either fex mutation alone is cryptic.

Chromosome Mapping↗
PubMed1981

Gene II of phage f1: its functions and its products.

Plasmids harboring the amino-terminal part of bacteriophage f1 gene II confer to bacterial cells partial resistance to infection with the male-specific bacteriophages f1 and f2. This effect (IP-2 phenotype) is due to the production of large amounts of an approximately 20,000-dalton polypeptide corresponding to the amino-terminal part of gene II protein. These results have allowed the isolation of clones producing functional gene II protein in large amounts. An in vitro assay has been developed to test the enzymatic activity of the gene II protein produced.

Cloning, Molecular↗
PubMed1979

Characterization of Op3, a lysis-defective mutant of bacteriophage f2.

We have isolated a conditional lethal mutant of bacteriophage 12 which makes plaques only on E. coli strains carrying a UGA suppressor. It grows normally in nonsuppressing hosts but does not lyse such strains. The mutation complements with amber mutations in each of the three known phage cistrons. These observations lead us to postulate the existence of a fourth gene in the RNA phage.

Amino Acids↗
PubMed1979

Organization of a hybrid between phage f1 and plasmid pSC101.

We have characterized the 200-nucleotide-long insertion found in f1 after segregation of a chimeric phage containing the genomes of f1 and pSC101 [Ohsumi, M., Vovis, G.F. & Zinder, N.D. (1978) Virology 89, 438--449]. The insertion in this novel f1 species, called f1', is derived from pSC101 and has the potential to form an extended base-paired secondary structure, as determined by nucleotide sequence analysis. A five-nucleotide direct repeat, derived from f1 sequences, is present in f1'. The 200 additional nucleotides that are inserted into the DNA sequence coding for the carboxy terminus of f1 gene IV protein have generated a novel carboxy terminus for the f1' gene IV protein. In vitro transcription--translation studies demonstrate that a read-through protein can be expressed, as predicted from the f1' nucleotide sequence results. This 200-nucleotide-long sequence appears to be a transposable element found within pSC101 and is similar in sequence to the inverted repeat found in Tn3. Restriction enzyme analysis of the chimeric phage DNA, coupled with the nucleotide sequencing results, allows us to predict a structure for the genomic organization of this chimera.

Base Sequence↗
PubMed1979

Insertion mutant of bacteriophage f1 sensitive to EcoRI.

The nucleotide sequence A-A-T-T was inserted into the intergenic region of the f1 genome at a site cleaved by Hae III (cleavage sequence (G-G-C-C). The resultant viable phage mutant (R199) contains a single site sensitive to the restriction endonuclease EcoRI (cleavage sequence G-A-A-T-T-C). This phage is sensitive to EcoRI restriction and modification in vivo and in vitro. Its potential for use as a cloning vector has been tested by construction in vitro of an f1/pBR322 chimeric phage. The four bases inserted into wild-type f1 to generate the R199 mutant came from a small restriction fragment obtained by digesting plasmid pBR322 with EcoRI and HindIII. The use of this linker prepared from a biological substrate is an example of a technique for constructing restriction enzyme sites in vitro. It is presented as an alternative to the use of synthetic linkers and should be generally applicable.

Base Sequence↗