Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.30.2 (endonuclease)
 18,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Inteins are protein-intervening sequences found inside the coding region of different host proteins and are translated in-frame with them. They can self-excise through protein splicing, which ligates the host protein flanks with a peptide bond. In this study, four different species of the genus Penicillium were investigated for the presence of inteins inside the conserved splicing-factor protein PRP8. We identified 157 to 162 amino acid in-frame insertions in the PRP8 protein of Penicillium chrysogenum, Penicillium expansum, and Penicillium vulpinum (formerly Penicillium claviforme). The Penicillium PRP8 inteins are mini-inteins without a conserved endonuclease domain. We demonstrated that the PRP8 mini-inteins of P. chrysogenum, P. expansum, and P. vulpinum undergo autocatalytic protein splicing when heterologously expressed in E. coli, in a model host protein, and in a divided GFP model system. They are, thus, among the smallest known nuclear-encoded, active splicing protein elements. The GFP assay should be valuable as a screening system for protein splicing inhibitors as potential antimycotic agents and as tools for studying the mechanism of protein splicing of fungal mini-inteins.
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PMID:Protein splicing of PRP8 mini-inteins from species of the genus Penicillium. 1654 41

Inteins are protein-intervening sequences that are translated with the host protein and can self-excise themselves post-translationally in an autocatalytic process. The flanking regions--called exteins--are then re-ligated with a new peptide bond, resulting in a mature host protein. Previously, we have identified inteins in the highly conserved 3.2 region of the PRP8 protein from species of the genus Penicillium. These inteins are integrated at the same position as that which has recently been described in PRP8 proteins from different strains of Cryptococcus neoformans and several ascomycetes. In this study, we investigated the presence of PRP8 inteins in four members of the genus Eupenicillium. Two species of this genus, Eupenicillium crustaceum and Eupenicillium baarnense, contain an intein at the same insertion site. Both inteins are mini-inteins and undergo self-splicing when heterologously expressed with a model host protein in Escherichia coli. Interestingly, we identified introns in the prp8-sequence encoding the 3.2 regions of the PRP8 protein in Eupenicillium meridianum and Eupenicillium terrenum. The introns are located 13 bps and 15 bps downstream of the putative intein insertion site. Here, we consider that the lack of inteins in these two species might be due to the prevention of endonuclease-mediated intein propagation in the intron-containing prp8-sequences.
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PMID:Inteins and introns within the prp8 -gene of four Eupenicillium species. 1925 33