Identification of a gene in Bacillus subtilis bacteriophage SPP1 determining the amount of packaged DNA

Tavares, Paulo; Santos, Mário A.; Lurz, Rudi; Morelli, Giovanna; Lencastre, Hermı́nia de; Trautner, Thomas A.

doi:10.1016/0022-2836(92)91027-m

Cited by 79 publications

(99 citation statements)

References 44 publications

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“…Full phage assembly is accomplished in the presence of gp6 Siz proteins, but the virions are defective because the short viral chromosome does not carry all the SPP1 essential genes. The siz mutations described here and by Tavares et al (1992) are found in different regions of gp6 primary structure (Fig. 5A).…”

Section: Characterization Of Gp6 Mutants Impaired In Dna Encapsidationmentioning

confidence: 58%

“…Phenotypes were grouped in five major classes: reduced accumulation of gp6 in the cell (rose), no gp6-gp7 interaction (black), deficiency of gp6 incorporation in the procapsid (variations in red indicate different severity of the phenotype; see Table 2), deficiency in DNA packaging (variations in blue) and undersizing of the mature DNA (variations in green). The position of siz mutations characterized previously (Tavares et al, 1992) and of the new locus sizI found in the present work is shown by vertical arrows. B. SPP1 morphogenetic pathway (adapted from Becker et al, 1997;Dröge et al, 2000;Orlova et al, 2003;Stiege et al, 2003).…”

Section: Achievement Of a Collection Of Gp6 Lethal Missense Mutantsmentioning

confidence: 59%

“…The mutation sizX causes an undersizing of the packaged DNA but does not interfere with assembly of infective virions (Tavares et al, 1992;1995). When strains bearing the gene 6 sizX allele are infected with SPP1 phages carrying a nonsense mutation in gene 6, the mature DNA detected has two distinct sizes as shown by PFGE (SizX , Fig.…”

Section: Mutations In Gp6 Leading To Dna Packaging Defectsmentioning

confidence: 99%

“…The portal protein is also involved in determination of the endonucleolytic cleavage that terminates DNA packaging. This role, initially described for phages that encapsidate DNA by a headful mechanism (Casjens et al ., 1992;Tavares et al ., 1992), was recently extended to bacteriophage l which terminates DNA packaging by a sequence-specific cleavage (Cue and Feiss, 1997).…”

Section: Introductionmentioning

confidence: 99%

“…Previous studies have shown that gp6 ensures the assembly of a procapsid structure with the correct size (Dröge et al ., 2000), that it targets the minor protein gp7 to the procapsid , that it modulates the ATPase activity of the terminase large subunit gp2 (Camacho et al ., 2003) and that it plays an essential role in the sizing of the DNA packaged (Tavares et al ., 1992). Gp6 has an overall architecture similar to that found for other portal proteins.…”

Section: Introductionmentioning

confidence: 99%

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The high‐resolution functional map of bacteriophage SPP1 portal protein

Isidro

Santos

Henriques

et al. 2003

Molecular Microbiology

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SummaryAn essential component in the assembly of nucleocapsids of tailed bacteriophages and of herpes viruses is the portal protein that is located at the unique vertex of the icosahedral capsid through which DNA movements occur. A library of mutations in the bacteriophage SPP1 portal protein (gp6) was generated by random mutagenesis of gene 6 . Screening of the library allowed identification of 67 single amino acid substitutions that impair portal protein function. Most of the mutations cluster within stretches of a few amino acids in the gp6 carboxyl-terminus. The mutations were divided into five classes according to the step of virus assembly that they impair: (1) production of stable gp6; (2) interaction of gp6 with the minor capsid protein gp7; (3) incorporation of gp6 in the procapsid structure; (4) DNA packaging; and (5) sizing of the packaged DNA molecule. Most of the mutations fell in classes 3 and 4. This is the first high-resolution functional map of a portal protein, in which its function at different steps of viral assembly can be directly correlated with specific regions of its sequence. The work provides a framework for the understanding of central processes in the assembly of viruses that use specialized portals to govern entry and exit of DNA from the viral capsid.

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Section: Characterization Of Gp6 Mutants Impaired In Dna Encapsidationmentioning

confidence: 58%

Section: Achievement Of a Collection Of Gp6 Lethal Missense Mutantsmentioning

confidence: 59%

Section: Mutations In Gp6 Leading To Dna Packaging Defectsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The high‐resolution functional map of bacteriophage SPP1 portal protein

Isidro

Santos

Henriques

et al. 2003

Molecular Microbiology

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2014

Beton und Stahlbetonbau

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DNA packaging and cutting by phage terminases: Control in phage T4 by a synaptic mechanism

Black

1995

BioEssays

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Phage DNA packaging occurs by DNA translocation into a prohead. Terminases are enzymes which initiate DNA packaging by cutting the DNA concatemer, and they are closely fitted structurally to the portal vertex of the prohead to form a 'packasome'. Analysis among a number of phages supports an active role of the terminases in coupling ATP hydrolysis to DNA translocation through the portal. In phage T4 the small terminase subunit promotes a sequence-specific terminase gene amplification within the chromosome. This link between recombination and packaging suggests a DNA synapsis mechanism by the terminase to control packaging initiation, formally homologous to eukaryotic chromosome segregation.

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Identification of a gene in Bacillus subtilis bacteriophage SPP1 determining the amount of packaged DNA

Cited by 79 publications

References 44 publications

The high‐resolution functional map of bacteriophage SPP1 portal protein

The high‐resolution functional map of bacteriophage SPP1 portal protein

PORR erhält drei Baulose im Wiener U‐Bahn‐Netz im Gesamtwert von 68 Mio. €

DNA packaging and cutting by phage terminases: Control in phage T4 by a synaptic mechanism

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