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At least 19 recordsLinked to original sources
PubMedDate not supplied

[Physicochemical characteristics of DNA and the amino acid composition of Bacillus phages].

From five Bacillus phages nucleic acids were isolated and identified as double-stranded DNA of the AT-type. Their melting point was 85-86.5 degrees C, molecular weight 23.4-43.7X10(6) daltons. The content of DNA in phage particles was 39.9-44.0%, the content of protein 55.7-56.1%. The examination of the amino acid composition in phages 125/50 and 617 revealed a low level of serine and the lack of methionine, while the remaining amino acid composition of Bacillus phages was close to that of E. coli T2 and T3 phages.

Amino Acids↗
PubMed2002

Effects of temperatures, pH-values, ultra-violet light, ethanol and chloroform on the growth of isolated thermophilic Bacillus phages.

Seven thermophilic Bacillus phages were characterized with reference to their host range, time of appearance, morphology of plaques, thermal inactivation, stability, lipid presence and inactivation by ultraviolet irradiation. Response surface methodology was adapted to describe the response of growth parameters to environmental changes. Most phages are susceptible to temperatures above 60 degrees C and inactivated immediately at 103 degrees C. Most phages are resistant to pH ranges 5 to 9 and almost all to pH 7 to 8. Both phages 46 and 80 were highly resistance to UV exposure for 13 minutes and 20 minutes, respectively. The presence of chloroform or 75% ethanol showed no effect on almost all isolated phages that indicate of possibility of the absence of lipids. The isolated phages were slow in their growth, possibly due to the lower gross growth efficiency.

Bacillus↗
PubMed1978

Partial characterization of a cubic Bacillus phage.

Partial characterization of a cubic Bacillus phage. Can. J. Microbiol. 24: 986--993. Phage Bam35 is an icosahedron of about 63 nm in diameter. It has a double capsid with spikes at the vertices, and a tail which seems to appear upon nucleic acid ejection. The phage contains DNA and, probably, lipids which seem to be located in the inner coat. The phage is Bacillus-specific, UV- and lipase-resistant, and sensitive to heat, chloroform, and ether. The latent period is 50 min and the burst size is 39. Page Bam35 belongs to a new virus group which includes a phage of B. anthracis and four phages of gram-negative bacteria harboring drug-resistance plasmids.

Bacillus thuringiensis↗
PubMed1987

Nucleotide sequence of Bacillus phage Nf terminal protein gene.

The nucleotide sequence of Bacillus phage Nf gene E has been determined. Gene E codes for phage terminal protein which is the primer necessary for the initiation of DNA replication. The deduced amino acid sequence of Nf terminal protein is approximately 66% homologous with the terminal proteins of Bacillus phages PZA and luminal diameter 29, and shows similar hydropathy and secondary structure predictions. A serine which has been identified as the residue which covalently links the protein to the 5' end of the genome in luminal diameter 29, is conserved in all three phages. The hydropathic and secondary structural environment of this serine is similar in these phage terminal proteins and also similar to the linking serine of adenovirus terminal protein.

Amino Acid Sequence↗
PubMed1986

Nucleotide sequence of gene F of Bacillus phage Nf.

The nucleotide sequence of Bacillus phage Nf gene F has been determined. The deduced amino acid sequence of gpF is very similar to that of gp4, the transcriptional activator of phage phi 29. Both proteins contain the consensus structure that is conserved for the DNA-protein interacting domain of DNA-binding proteins such as the repressor, Cro and CII proteins of phage lambda.

Amino Acid Sequence↗
PubMed1986

Nucleotide sequence of Bacillus phage phi 29 genes 14 and 15: homology of gene 15 with other phage lysozymes.

The nucleotide sequence of Bacillus phage phi 29 genes 14 (g14) and 15 (g15) have been determined and shown to encode proteins with molecular weights of 15,014 and 28,022, respectively. The g14 open reading frame (ORF) was confirmed by sequencing a sus14(1241) mutant. Gene product 15 (gp15) has considerable homology with Salmonella phage P22 lysozyme and lesser homology with Escherichia coli phage T4 lysozyme. Putative translation signals are identified. In addition, the role of a previously described promoter, B2, is discussed.

Amino Acid Sequence↗
PubMed1997

Bacteriophage B103: complete DNA sequence of its genome and relationship to other Bacillus phages.

The genome of Bacillus subtilis bacteriophage B103 consists of double-stranded linear DNA 18,630 bp long. The DNA was sequenced, and the sequence was compared with DNA sequences of closely related phages, namely the members of the phage phi29 family. Among them, phage Nf was shown to be the most closely related to B103. Comparisons of several open reading frames (ORFs) among the family members helped to identify genes 1 and 5. A cluster of ORFs between genes 16 and 17 contains two ORFs with partial homology with two phi29 ORFs located in the same region. There are three more ORFs in this region of B103 with good ribosome binding sites (RBS) and optimal codon usage that are not homologous to any of the phi29 ORFs. The function of these five ORFs remains unexplained. It was shown that major promoters characterized in phi29 are retained in B103. Where many substitutions occur in the vicinity of a promoter, at least the -10 and -35 boxes are conserved.

Amino Acid Sequence↗
PubMed1986

The nucleotide sequences of the heterologous region between the genomes of Bacillus phages M2 and Nf that indicate the two phages are originally identical.

It has been suggested that the heterologous population of Bacillus phage M2 is derived from an original clone, which is identical with phage Nf, by the deletion on a particular region of the genome. We have determined the nucleotide sequence of this region of M2 subclones and Nf genomes. The results clearly indicate that the homologous recombination through the short direct repeated sequence is the main cause of the varied deletions found in the genomes of M2 subclones.

Bacillus↗
PubMed1986

Nucleotide sequence of the late region of Bacillus phage phi 29 completes the 19,285-bp sequence of phi 29 genome. Comparison with the homologous sequence of phage PZA.

The 12,177-bp nucleotide (nt) sequence of the late region of Bacillus phage luminal diameter 29 genome was determined. This sequence completes the entire 19,285-bp sequence of phage luminal diameter 29 DNA. Eleven open reading frames were found in this region, and these were assigned to eleven late genes. Ribosome-binding sites and a potential transcriptional promoter and terminator are considered. The nt sequence was compared to the homologous region of the closely related phage PZA and tolerated variations at the nt and amino acid (aa) level were evaluated. The most frequent changes are silent nt substitutions in the third position of codons, but aa substitutions are also found.

Bacteriophages↗
PubMed1985

The complete sequence of the Bacillus phage phi 29 right early region.

We have sequenced the rightmost 2216 bp of the Bacillus phage phi 29 genome. This region encompasses the right early region and completes the sequence of the phi 29 early functions. The sequence of gene 17, an early gene implicated in the replication process, is presented. From these results we predict that gene 17 encodes a 19.1-kDal protein. Further analysis of the sequence revealed five previously undetected potential genes, encoding 12.6-, 12.4-, 15.2-, 6.2- and 4.6-kDal proteins. The biological efficacies of some of these putative genes were demonstrated using an Escherichia coli in vitro transcription-translation system. We also examined the transcriptional and translational signals present on this region of the genome.

Amino Acid Sequence↗
PubMed1985

The complete sequence of Bacillus phage phi 29 gene 16: a protein required for the genome encapsidation reaction.

We have sequenced the region of the Bacillus phage phi 29 genome that encodes gene 16, the gene product of which catalyzes the in vivo and in vitro genome-encapsidation reaction. The identity of the coding frame was confirmed by sequencing a sus mutant, sus16(300). It is concluded that gene 16 encodes a 39-kDal protein and is comprised of 331 amino acids. Only 30 bp separates gene 16 from the last open reading frame of the right early region. Analysis of potential secondary structures in this region suggests that the same sequences may be involved in the termination of both the late and early transcripts.

Amino Acid Sequence↗
PubMed1989

Nucleotide sequence of the right early region of Bacillus phage phi 15 and comparison with related phages: reorganization of gene 17 during evolution.

The rightmost 2016 bp of the Bacillus subtilis phage phi 15 genome were sequenced. The nucleotide sequence was compared with the homologous regions of the related phages PZA and phi 29. There are six open reading frames (ORFs) in this region of the phi 15 genome; all of them are present in the PZA and phi 29 genomes. One of the ORFs was assigned to gene 17, which is involved in the replication of the phage DNA. Gene 17 has undergone reorganization during the evolution of this phage family. Comparison of the nucleotide sequence of its mRNA-like strand in phi 15, PZA and phi 29 showed that deletions in its central and 3'-end-proximal parts are tolerated and do not interfere with the gene 17 product function. It seems that the only portion of gene 17 that has to be conserved to encode the functional product is its 5'-end-proximal part.

Amino Acid Sequence↗
PubMed2004

Group I intron homing in Bacillus phages SPO1 and SP82: a gene conversion event initiated by a nicking homing endonuclease.

Many group I introns encode endonucleases that promote intron homing by initiating a double-stranded break-mediated homologous recombination event. In this work we describe intron homing in Bacillus subtilis phages SPO1 and SP82. The introns encode the DNA endonucleases I-HmuI and I-HmuII, respectively, which belong to the H-N-H endonuclease family and possess nicking activity in vitro. Coinfections of B. subtilis with intron-minus and intron-plus phages indicate that I-HmuI and I-HmuII are required for homing of the SPO1 and SP82 introns, respectively. The homing process is a gene conversion event that does not require the major B. subtilis recombination pathways, suggesting that the necessary functions are provided by phage-encoded factors. Our results provide the first examples of H-N-H endonuclease-mediated intron homing and the first demonstration of intron homing initiated by a nicking endonuclease.

Bacillus Phages↗
PubMed1985

[Effect of the pC194 plasmid on the development of Bacillus thuringiensis phages].

Bacillus thuringiensis var. galleriae strains were transformed by plasmid pC194, coding for chloramphenicol resistance (CmR). Efficiency of plating and the yields of bacteriophages Tg13 and Tg27 maturating in CmR transformant cells were decreased for 2-3 orders as compared with the ones in parental strains. The CmR transformants are characterized by the increased level of spontaneous induction of bacteriophage Tg22.

Bacillus thuringiensis↗
PubMed1980

Specificity of promoter site utilization in vitro by bacterial RNA polymerases on Bacillus phage phi 29 DNA. Transcription mapping with exonuclease III.

Bacillus subtilis RNA polymerase holoenzyme transcribes phi 29 DNA in vitro producing five major RNA species defined by characteristic electrophoretic mobilities. In addition to these products, Escherichia coli RNA polymerase transcribes phi 29 DNA to yield three RNA species not detected when transcribing with the B. subtilis enzyme under the same optimal reaction conditions for RNA synthesis. Transcriptional analysis of purified restriction fragments and exonuclease III-digested DNA established locations of six promoter and three termination sites defining the eight transcripts. The transcription map shows that E. coli RNA polymerase initiates transcription at three sites not efficiently utilized by the B. subtilis enzyme. However, initiation by the B. subtilis polymerase from at least two of these sites could be detected at E:DNA ratios greater than 10 in the absence of competing promoters. These results indicate that differences between the two polymerases in promoter utilization are not explained by specificity of promoter binding, but represent differences in responding to promoter strength. Transcription of phi 29 DNA and T7 DNA by E. coli core polymerase with either B. subtilis or E. coli sigma subunits results in formation of transcripts identical with those produced by E. coli holoenzyme, suggesting that core polymerase contains elements important in determining relative promoter strength. The efficiency of rifampicin-resistant complex formation on phi 29 and T7 promoters is also dependent upon the source of core polymerase.

Bacillus subtilis↗