Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-2-20
pubmed:abstractText
Deoxyribonuclease IIalpha (DNase IIalpha) is an acidic endonuclease found in lysosomes and nuclei, and it is also secreted. Though its Caenorhabditis elegans homolog, NUC-1, is required for digesting DNA of apoptotic cell corpses and dietary DNA, it is not required for viability. However, DNase IIalpha is required in mice for correct development and viability, because undigested cell corpses lead to lesions throughout the body. Recently, we showed that, in contrast to previous reports, active DNase IIalpha consists of one contiguous polypeptide. To better analyze DNase II protein structure and determine residues important for activity, extensive database searches were conducted to find distantly related family members. We report 29 new partial or complete homologs from 21 species. Four homologs with differences at the purported active site histidine residue were detected in the parasitic nematodes Trichinella spiralis and Trichinella pseudospiralis. When these mutations were reconstructed in human DNase IIalpha, the expressed proteins were inactive. DNase II homologs were also identified in non-metazoan species. In particular, the slime-mold Dictyostelium, the protozoan Trichomonas vaginalis, and the bacterium Burkholderia pseudomallei all contain sequences with significant similarity and identity to previously cloned DNase II family members. We report an analysis of their sequences and implications for DNase II protein structure and evolution.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
305
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-12
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12594037-Amino Acid Sequence, pubmed-meshheading:12594037-Animals, pubmed-meshheading:12594037-Binding Sites, pubmed-meshheading:12594037-Blotting, Western, pubmed-meshheading:12594037-Burkholderia pseudomallei, pubmed-meshheading:12594037-Cells, Cultured, pubmed-meshheading:12594037-Conserved Sequence, pubmed-meshheading:12594037-Databases, Genetic, pubmed-meshheading:12594037-Endodeoxyribonucleases, pubmed-meshheading:12594037-Expressed Sequence Tags, pubmed-meshheading:12594037-Fibroblasts, pubmed-meshheading:12594037-Genome, pubmed-meshheading:12594037-Histidine, pubmed-meshheading:12594037-Humans, pubmed-meshheading:12594037-Mice, pubmed-meshheading:12594037-Molecular Sequence Data, pubmed-meshheading:12594037-Mutation, pubmed-meshheading:12594037-Phylogeny, pubmed-meshheading:12594037-Plasmids, pubmed-meshheading:12594037-Sequence Alignment, pubmed-meshheading:12594037-Sequence Homology, Amino Acid, pubmed-meshheading:12594037-Species Specificity, pubmed-meshheading:12594037-Transfection, pubmed-meshheading:12594037-Trichinella spiralis
pubmed:year
2003
pubmed:articleTitle
A family history of deoxyribonuclease II: surprises from Trichinella spiralis and Burkholderia pseudomallei.
pubmed:affiliation
Department of Pharmacology and Toxicology, Dartmouth Medical School, 7650 Remsen, Hanover, NH 03755, USA
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.