Linked Life Data

8577256

Source:http://linkedlifedata.com/resource/pubmed/id/8577256

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1996-3-12
pubmed:databankReference
pubmed:abstractText
Listeria monocytogenes bacteriophages A118, A500 and A511 are members of three distinct phage groups with characteristic host ranges. Their endolysin (ply) genes were cloned and expressed in Escherichia coli as demonstrated by the conferred lytic phenotype when colonies of recombinant cells were overlaid with a lawn of Listeria cells. The nucleotide sequences of the cloned DNA fragments were determined and the individual enzymes (PLY118, 30.8 kDa; PLY500, 33.4 kDa; PLY511, 36.5 kDa) were shown to have varying degrees of homology within their N-terminal or C-terminal domains. Transcriptional analysis revealed them to be 'late' genes with transcription beginning 15-20 min post-infection. The enzymes were overexpressed and partially purified and their individual specificities examined. When applied exogenously, the lysins induced rapid lysis of Listeria strains from all species but generally did not affect other bacteria. Using hydrolysis of purified listerial cell walls, PLY511 was characterized as an N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) and shows homology in its N-terminal domain to other enzymes of this type. In contrast, PLY118 and PLY500 were shown to represent a new class of cell wall lytic enzymes which cleave between the L-alanine and D-glutamate residues of listerial peptidoglycan; these were designated as L-alanoyl-D-glutamate peptidases. These two enzymes share homology in the N-terminal domain which we propose determines hydrolytic specificity. Highly conserved holin (hol) gene sequences are present upstream of ply118 and ply500. They encode proteins of structural similarity to the product of phage lambda gene S, and are predicted to be membrane proteins which form pores to allow access of the lysins to their peptidoglycan substrates. This arrangement of conserved holin genes with downstream lysin genes among the siphoviral lysis cassettes explains why the cytoplasmic endolysins alone are not lethal, since they require a specific transport function across the cell membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1231-41
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8577256-Amino Acid Sequence, pubmed-meshheading:8577256-Bacteriolysis, pubmed-meshheading:8577256-Base Sequence, pubmed-meshheading:8577256-Carbohydrate Sequence, pubmed-meshheading:8577256-Cloning, Molecular, pubmed-meshheading:8577256-Endopeptidases, pubmed-meshheading:8577256-Gene Expression, pubmed-meshheading:8577256-Genes, Viral, pubmed-meshheading:8577256-Genotype, pubmed-meshheading:8577256-Listeria monocytogenes, pubmed-meshheading:8577256-Molecular Sequence Data, pubmed-meshheading:8577256-N-Acetylmuramoyl-L-alanine Amidase, pubmed-meshheading:8577256-Recombinant Proteins, pubmed-meshheading:8577256-Sequence Alignment, pubmed-meshheading:8577256-Sequence Analysis, pubmed-meshheading:8577256-Siphoviridae, pubmed-meshheading:8577256-Substrate Specificity, pubmed-meshheading:8577256-Viral Proteins
pubmed:year
1995
pubmed:articleTitle
Heterogeneous endolysins in Listeria monocytogenes bacteriophages: a new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes.
pubmed:affiliation
Institut für Mikrobiologie, Technische Universität München, Freising, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't