Back to Search
Start Over
A new class of tetraspanins in fungi.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2002 Oct 11; Vol. 297 (5), pp. 1197-204. - Publication Year :
- 2002
-
Abstract
- Tetraspanins are animal proteins involved in membrane complexes that are involved in cell adhesion, differentiation, and motility. The PLS1 gene from rice blast fungus Magnaporthe grisea encodes a protein (Pls1p) structurally related to tetraspanins that is required for pathogenicity. In Botrytis cinerea public sequences, we identified an EST homologous to PLS1. Using degenerated oligonucleotides, we amplified sequences homologous to PLS1 in fungi Colletotrichum lindemuthianum and Neurospora crassa. Analysis of N. crassa and M. grisea genome sequences revealed the presence of a single tetraspanin gene. Thus, fungi differ from animals, which contain between 20 and 37 paralogous tetraspanin genes. Fungal proteins encoded by BcPLS1, ClPLS1, and NcPLS1 display all the structural hallmarks of tetraspanins (predicted topology with four transmembrane domains, extra- and intracellular loops; conserved cysteine-based patterns in second extracellular loop). Phylogenetic analysis suggests that these genes define a new family of orthologous genes encoding fungal-specific tetraspanins.
- Subjects :
- Amino Acid Sequence
Blotting, Southern
Botrytis metabolism
Cloning, Molecular
DNA, Complementary metabolism
Exons
Expressed Sequence Tags
Fungal Proteins classification
Fungal Proteins genetics
Introns
Magnaporthe metabolism
Molecular Sequence Data
Neurospora crassa metabolism
Phylogeny
Polymerase Chain Reaction
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Software
Fungal Proteins chemistry
Fungi metabolism
Membrane Proteins chemistry
Membrane Proteins classification
Membrane Proteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 297
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 12372414
- Full Text :
- https://doi.org/10.1016/s0006-291x(02)02355-0