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Zoocin A is a domain-structured peptidoglycan hydrolase produced by Streptococcus equi ssp. zooepidemicus 4881. [¹⁴C]-zoocin A was used to measure the amount of zoocin A bound to the surface of cells and to purified peptidoglycan. The sensitivity of various streptococci to zoocin A correlated with the amount of zoocin A bound (R²=0.8609). Peptidoglycan purified from Streptococcus oralis and Streptococcus rattus were able to bind zoocin A but remained resistant to hydrolysis. All Streptococcus pyogenes strains were extremely sensitive to zoocin A with minimum inhibition concentrations of 31.5 ng mL⁻¹ or less, suggesting that zoocin A may have potential for use as an enzybiotic.

In Rehearsal is a clear and accessible how-to approach to the rehearsal process. Author Gary Sloan brings more than thirty years' worth of acting experience to bear on the question of how to rehearse both as an individual actor and as part of the team of professionals that underpins any successful production. Interviews with acclaimed actors, directors, playwrights, and designers share a wealth of knowledge on dynamic collaboration. The book is divided in to three main stages, helping the reader to refine their craft in as straightforward and accessible manner as possible: In the world: A flexible rehearsal program that can be employed daily, as well as over a typical four week production rehearsal. In the room: Advice on working independently and productively with other members of a company, such as directors, playwrights, designers and technical crew; how your personal creative process varies depending on the role, be it Shakespeare, musicals, film, television or understudying. On your own: Creating your own rehearsal process, exploring original and famous rehearsal techniques, breaking through actor's block and how to practice every day. In Rehearsal breaks down the rehearsal process from the actor's perspective and equips its reader with the tools to become a generous and resourceful performer both inside and outside the studio. Its independent, creative and daily rehearsal techniques are essential for any modern actor.

In Rehearsal is a clear and accessible how-to approach to the rehearsal process. Author Gary Sloan brings more than thirty years' worth of acting experience to bear on the question of how to rehearse both as an individual actor and as part of the team of professionals that underpins any successful production. Interviews with acclaimed actors, directors, playwrights, and designers share a wealth of knowledge on dynamic collaboration. The book is divided in to three main stages, helping the reader to refine their craft in as straightforward and accessible manner as possible: In the world: A flexible rehearsal program that can be employed daily, as well as over a typical four week production rehearsal. In the room: Advice on working independently and productively with other members of a company, such as directors, playwrights, designers and technical crew; how your personal creative process varies depending on the role, be it Shakespeare, musicals, film, television or understudying. On your own: Creating your own rehearsal process, exploring original and famous rehearsal techniques, breaking through actor's block and how to practice every day. In Rehearsal breaks down the rehearsal process from the actor's perspective and equips its reader with the tools to become a generous and resourceful performer both inside and outside the studio. Its independent, creative and daily rehearsal techniques are essential for any modern actor.

Zoocin A is a streptococcolytic enzyme produced by Streptococcus equi subsp. zooepidemicus strain 4881. The zoocin A gene (zooA) and the gene specifying resistance to zoocin A (zif) are adjacent on the chromosome and are divergently transcribed. Twenty-four S. equi subsp. zooepidemicus strains were analyzed to determine the genetic difference among three previously characterized as zoocin A producers (strains 4881, 9g, and 9h) and the 21 nonproducers. LT-PCR and Southern hybridization studies revealed that none of the nonproducer strains possessed zooA or zif. RAPD and PFGE showed that the 24 strains were a genetically diverse population with eight RAPD profiles. S. equi subsp. zooepidemicus strains 9g and 9h appeared to be genetically identical to each other but quite different from strain 4881. Sequences derived from 4881 and 9g showed that zooA and zif were integrated into the chromosome adjacent to the gene flaR. A comparison of these sequences with the genome sequences of S. equi subsp. zooepidemicus strains H70 and MGCS10565 and S. equi subsp. equi strain 4047 suggests that flaR flanks a region of genome plasticity in this species.

Zoocin A is a streptococcolytic enzyme produced by Streptococcus equi subsp. zooepidemicus 4881 that has an unknown site of action on the peptidoglycans of susceptible organisms. Analysis of a mutant strain in which the genes for zoocin A and resistance to zoocin A were inactivated revealed that this strain was more susceptible to β-lactam antibiotics than the parental organism. Purified zoocin A had weak β-lactamase activity, bound radioactive penicillin covalently, and its streptococcolytic activity was inhibited by penicillin. Thus, zoocin A is a penicillin-binding protein and presumably is a d-alanyl endopeptidase.

A plasmid from Staphylococcus sciuri DD 4747 had three open reading frames: a replication gene, an N-acetylmuramyl- l-alanine amidase-like gene, and a gene similar to the lysostaphin endopeptidase resistance gene ( epr/ lif). The epr-like gene was introduced into S. aureus RN4220; the recombinant strain was more resistant to lysostaphin endopeptidase and its cell wall peptidoglycan contained more serines and fewer glycines than the parental strain with the shuttle vector alone. Based on both its function and its similarity to femAB, this gene is a member of the femABX-like immunity gene family. Furthermore, this is the first example of a femABX-like immunity gene that is not linked to the gene for the bacteriolytic enzyme against which it specifies immunity.

To determine if the genes for lysostaphin endopeptidase ( end) and lysostaphin resistance ( epr) function in streptococci, we transferred these genes from Staphylococcus simulans biovar staphylolyticus into two strains of Streptococcus equi subsp. zooepidemicus. The end-containing streptococci were able to produce and process proendopeptidase. Strains containing epr were more resistant to lysis by the streptococcolytic enzyme zoocin A and amino acid analysis of the peptidoglycans of the epr-containing streptococci revealed insertion of serines in their cross bridges. This is the first report of the transfer of a femABX-like immunity factor resulting in a physiologically useful effect in a different genus.

A 6.8-kb fragment of Streptococcus equi subsp. zooepidemicus 4881 DNA containing the zoocin A gene ( zooA) was cloned in Escherichia coli and sequenced. We have identified a gene we call zoocin A immunity factor ( zif), which protects the producer cell from the otherwise lethal action of its own product. Transformation of Streptococcus gordonii DL1 with zooA and zif changed its phenotypic character from a non-zoocin A producing-zoocin A sensitive cell to a zoocin A producing-zoocin A resistant cell. zif has sequence homology to femA (factor essential for methicillin resistance) and lif (lysostaphin immunity factor). No differences were observed in amino acid or amino sugar compositions of peptidoglycan purified from zoocin A sensitive vs. zoocin A immune cells.

Staphylococcus simulans biovar staphylolyticus produces a staphylolytic glycylglycine endopeptidase (lysostaphin) and a micrococcolytic endo-β- N-acetylglucosaminidase (hexosaminidase) as proenzymes that are proteolytically processed through multiple intermediates to their mature forms by an extracellular sulfhydryl protease. Analysis of protease production by immunoblots using antiserum prepared against purified protease and by renaturing activity gels using gelatin as the substrate has revealed that the lysostaphin-processing protease also is produced as a proenzyme, which appears to be autocatalytically processed. Very little proprotease could be detected in supernatants from cultures of S. simulans biovar staphylolyticus, which suggested that the protein was being processed before it was released to the culture medium. Analysis of wall-associated proteins revealed that processing of proprotease occurred primarily in the cell wall. Furthermore, processing of prolysostaphin and prohexosaminidase also occurred in the cell wall matrix.