Rz/Rz1 Lysis Gene Equivalents in Phages of Gram-negative Hosts

Summer, Elizabeth J.; Berry, Joel D.; Tran, Tri M.; Niu, Lili; Struck, Douglas K.; Young, Ry

doi:10.1016/j.jmb.2007.08.045

Cited by 142 publications

(203 citation statements)

References 48 publications

Supporting

Mentioning

199

Contrasting

Order By: Relevance

“…The predicted N-terminal TMD and a-helical regions are highlighted and underlined, respectively. 8 The region of Rz deleted during the construction of pSRzH 6 (see ''Materials and methods'') is indicated by a cross bar and D symbol. The sequence and location of the C-terminal oligohistidine tag are also indicated.…”

Section: Purification Of the Rz And Rz1 Periplasmic Domainsmentioning

confidence: 99%

“…Both topology and genetics mandate that this interaction occurs via the C-termini of both proteins. 1,8 Evidence that this interaction occurs in vivo was obtained by assessing the state of the full-length Rz protein in whole cells in which the Rz gene was expressed at physiological levels ( Fig. 5).…”

Section: The Rz Protein Is Stabilized By Rz1 In Vivomentioning

confidence: 99%

“…6,7 Aided by the striking architecture, which is unique in biology for two genes involved in the same function, we identified equivalents of Rz-Rz1 in nearly all genomes of phages that infect Gram-negative bacteria. 8 The ubiquity and diversity (37 unrelated gene families) suggested that, for phage lysis, Rz and Rz1 are just as important as holins and endolysins.…”

Section: Introductionmentioning

confidence: 99%

“…1(A)]. 8 The mature Rz1 protein is a 40 residue OM lipoprotein containing 10 Pro residues and devoid of predicted secondary structure [ Fig. 1(B)].…”

Section: Introductionmentioning

confidence: 99%

“…1(B)]. 8,10 Multiple lines of genetic, physiological, and molecular evidence suggest that Rz and Rz1 form a complex, which, as it must span the periplasm, has been designated as the spanin complex. According to this formalism, Rz and Rz1 are the large and small spanin subunits, respectively.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation

et al. 2010

Self Cite

View full text Add to dashboard Cite

Phage holins and endolysins have long been known to play key roles in lysis of the host cell, disrupting the cytoplasmic membrane and peptidoglycan (PG) layer, respectively. For phages of Gram-negative hosts, a third class of proteins, the spanins, are involved in disrupting the outer membrane (OM). Rz and Rz1, the components of the lambda spanin, are, respectively, a class II inner membrane protein and an OM lipoprotein, are thought to span the entire periplasm by virtue of C-terminal interactions of their soluble domains. Here, the periplasmic domains of Rz and Rz1 have been purified and shown to form dimeric and monomeric species, respectively, in solution. Circular dichroism analysis indicates that Rz has significant alpha-helical character, but much less than predicted, whereas Rz1, which is 25% proline, is unstructured. Mixture of the two proteins leads to complex formation and an increase in secondary structure, especially alpha-helical content. Moreover, transmission electron-microscopy reveals that Rz-Rz1 complexes form large rod-shaped structures which, although heterogeneous, exhibit periodicities that may reflect coiledcoil bundling as well as a long dimension that matches the width of the periplasm. A model is proposed suggesting that the formation of such bundles depends on the removal of the PG and underlies the Rz-Rz1 dependent disruption of the OM.

show abstract

Section: Purification Of the Rz And Rz1 Periplasmic Domainsmentioning

confidence: 99%

Section: The Rz Protein Is Stabilized By Rz1 In Vivomentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…1(A)]. 8 The mature Rz1 protein is a 40 residue OM lipoprotein containing 10 Pro residues and devoid of predicted secondary structure [ Fig. 1(B)].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation

et al. 2010

Self Cite

View full text Add to dashboard Cite

show abstract

Phage Genome Annotation Using the RAST Pipeline

McNair

Aziz

Pusch

et al. 2017

Methods in Molecular Biology

View full text Add to dashboard Cite

Phages are complex biomolecular machineries that have to survive in a bacterial world. Phage genomes show many adaptations to their lifestyle such as shorter genes, reduced capacity for redundant DNA sequences, and the inclusion of tRNAs in their genomes. In addition, phages are not free-living, they require a host for replication and survival. These unique adaptations provide challenges for the bioinformatics analysis of phage genomes. In particular, ORF calling, genome annotation, noncoding RNA (ncRNA) identification, and the identification of transposons and insertions are all complicated in phage genome analysis. We provide a road map through the phage genome annotation pipeline, and discuss the challenges and solutions for phage genome annotation as we have implemented in the rapid annotation using subsystems (RAST) pipeline.

show abstract

The temperate Burkholderia phage AP3 of the Peduovirinae shows efficient antimicrobial activity against B. cenocepacia of the IIIA lineage

Roszniowski

Łątka

Maciejewska

et al. 2016

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Burkholderia phage AP3 (vB_BceM_AP3) is a temperate virus of the Myoviridae and the Peduovirinae subfamily (P2likevirus genus). This phage specifically infects multidrug-resistant clinical Burkholderia cenocepacia lineage IIIA strains commonly isolated from cystic fibrosis patients. AP3 exhibits high pairwise nucleotide identity (61.7 %) to Burkholderia phage KS5, specific to the same B. cenocepacia host, and has 46.7–49.5 % identity to phages infecting other species of Burkholderia. The lysis cassette of these related phages has a similar organization (putative antiholin, putative holin, endolysin, and spanins) and shows 29–98 % homology between specific lysis genes, in contrast to Enterobacteria phage P2, the hallmark phage of this genus. The AP3 and KS5 lysis genes have conserved locations and high amino acid sequence similarity. The AP3 bacteriophage particles remain infective up to 5 h at pH 4–10 and are stable at 60 °C for 30 min, but are sensitive to chloroform, with no remaining infective particles after 24 h of treatment. AP3 lysogeny can occur by stable genomic integration and by pseudo-lysogeny. The lysogenic bacterial mutants did not exhibit any significant changes in virulence compared to wild-type host strain when tested in the Galleria mellonella moth wax model. Moreover, AP3 treatment of larvae infected with B. cenocepacia revealed a significant increase (P < 0.0001) in larvae survival in comparison to AP3-untreated infected larvae. AP3 showed robust lytic activity, as evidenced by its broad host range, the absence of increased virulence in lysogenic isolates, the lack of bacterial gene disruption conditioned by bacterial tRNA downstream integration site, and the absence of detected toxin sequences. These data suggest that the AP3 phage is a promising potent agent against bacteria belonging to the most common B. cenocepacia IIIA lineage strains.Electronic supplementary materialThe online version of this article (doi:10.1007/s00253-016-7924-7) contains supplementary material, which is available to authorized users.

show abstract

Rz/Rz1 Lysis Gene Equivalents in Phages of Gram-negative Hosts

Cited by 142 publications

References 48 publications

The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation

The lambda spanin components Rz and Rz1 undergo tertiary and quaternary rearrangements upon complex formation

Phage Genome Annotation Using the RAST Pipeline

The temperate Burkholderia phage AP3 of the Peduovirinae shows efficient antimicrobial activity against B. cenocepacia of the IIIA lineage

Contact Info

Product

Resources

About