Structure of phage P22 gene 19 lysozyme inferred from its homology with phage T4 lysozyme

Weaver, L.H.; Rennell, Dale; Poteete, Anthony R.; Matthews, Brian W.

doi:10.1016/0022-2836(85)90318-3

Cited by 21 publications

(15 citation statements)

References 13 publications

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“…171,1989 on May 12, 2018 by guest http://jb.asm.org/ Downloaded from to suggest that they diverged from a common evolutionary precursor (Table 1). It was also suggested that the structure of the phage P22 lysozyme provides an evolutionary link between phage T4 lysozyme and GEWL (61).…”

Section: Criteria Used To Infer Common Ancestrymentioning

confidence: 99%

Bacteriophage T4 genetic homologies with bacteria and eucaryotes

Bernstein

1989

J Bacteriol

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Section: Criteria Used To Infer Common Ancestrymentioning

confidence: 99%

Bacteriophage T4 genetic homologies with bacteria and eucaryotes

Bernstein

1989

J Bacteriol

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“…The P22 lysozyme sequence is easily aligned with that of the T4 lysozyme (T4L) and its structure has been modeled on the T4L pattern (Weaver et al, 1985b). This led us to analyse the evolutionary relationship between λL and V-type lysozymes using multiple sequence alignments, secondary structure predictions and pattern recognition methods.…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes

Evrard

Fastrez

Declercq

1998

Journal of Molecular Biology

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Like other lysozymes, the bacteriophage lambda lysozyme is involved in the digestion of bacterial walls. This enzyme is remarkable in that its mechanism of action is different from the classical lysozyme's mechanism. From the point of view of protein evolution, it shows features of lysozymes from different classes.The crystal structure of the enzyme in which all tryptophan residues have been replaced by aza-tryptophan has been solved by X-ray crystallography at 2.3 Å using a combination of multiple isomorphous replacement, noncrystallographic symmetry averaging and density modification techniques. There are three molecules in the asymmetric unit. The characteristic structural elements of lysozymes are conserved: each molecule is organized in two domains connected by a helix and the essential catalytic residue (Glu19) is located in the depth of a cleft between the two domains. This cleft shows an open conformation in two of the independent molecules, while access to the cavity is much more restricted in the last one. A structural alignment with T4 lysozyme and hen egg white lysozyme allows us to superpose about 60 C α atoms with a rms distance close to 2 Å. The best alignments concern the helix preceding the catalytic residue, some parts of the β sheets and the helix joining the two domains. The results of sequence alignments with the V and C lysozymes, in which weak local similarities had been detected, are compared with the structural results.

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“…These techniques exploit properties of P22-lysogeny, relative simplicity of lysis functions, and DNA that can be cut with restriction endonucleases-that are not shared by T4. P22 lysozyme is functionally interchangeable with T4 lysozyme and is thought to be structurally similar to it (14,17). Our greater knowledge of the T4 lysozyme structure, however, makes it a better object than P22 lysozyme for structural studies.…”

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confidence: 99%

Mutations in an upstream regulatory sequence that increase expression of the bacteriophage T4 lysozyme gene

et al. 1987

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A P22 hybrid phage bearing the bacteriophage T4 lysozyme gene (e), as well as T4 sequences upstream from the lysozyme gene, was constructed. Amber mutations were introduced into gene e in the hybrid phage, and the resulting mutant phages were tested for the ability to form plaques on amber suppressor strains. Revertant phages that were able to form plaques on amber suppressors that did not suppress the parent amber mutant phages were isolated following UV mutagenesis. Secondary site pseudorevertants were identified among the revertants by a genetic test. Four of the suppressing secondary site mutations were mapped and sequenced. They were found to consist of small sequence alterations immediately upstream from gene e, all of which would tend to destabilize potential base-pairing interactions in the transcript. The mutations were shown to increase lysozyme expression when introduced into an otherwise wild-type hybrid phage, but were found to have little effect on transcription of the lysozyme gene.Bacteriophage lysozymes are exceptionally well suited for structural studies involving mutant variants. The lysozyme of bacteriophage T4 has been investigated the most intensively (5, 13). With the aim of generating structurally altered lysozymes, we have recently developed techniques for systematically introducing mutations into the phage P22 lysozyme gene, crossing them into phage, and isolating secondary site revertants (D. Rennell and A. R. Poteete, unpublished data). These techniques exploit properties of P22-lysogeny, relative simplicity of lysis functions, and DNA that can be cut with restriction endonucleases-that are not shared by T4. P22 lysozyme is functionally interchangeable with T4 lysozyme and is thought to be structurally similar to it (14, 17). Our greater knowledge of the T4 lysozyme structure, however, makes it a better object than P22 lysozyme for structural studies. For this reason, we sought to develop methods for working with T4 lysozyme in a hybrid P22 phage in which it substitutes for the P22 lysozyme.The hybrid phage that we constructed includes the T4 lysozyme gene (e) and 75 base pairs (bp) of T4 DNA upstream from it. We introduced mutations into gene e and selected secondary site revertants; some of these revertants were found to have secondary mutations in the upstream sequence. Perry et al. (11) regulatory structure, and result in increased expression of lysozyme. These results provide genetic evidence for the involvement of base pairing in the upstream sequence in the regulation of lysozyme expression. In this report, we describe the isolation and characterization of the mutants. MATERIALS AND METHODSPlasmids. Plasmids pTP30, pDR100, and pDR11O have been described previously (1,14). Plasmid constructions were done by standard methods (7), with pBR322 (2) used as the vector. Details of particular constructions are given in Table 1.Plasmid pMS421 contains the Escherichia coli lacI repressor gene and determinants for resistance to spectinomycin and streptomycin (M. Susskind and A. R. Poteet...

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Structure of phage P22 gene 19 lysozyme inferred from its homology with phage T4 lysozyme

Cited by 21 publications

References 13 publications

Bacteriophage T4 genetic homologies with bacteria and eucaryotes

Bacteriophage T4 genetic homologies with bacteria and eucaryotes

Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes

Mutations in an upstream regulatory sequence that increase expression of the bacteriophage T4 lysozyme gene

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