20682355
not annotated - annotated - LINNAEUS only
PRP8 intein in Ajellomycetaceae family pathogens: sequence analysis, splicing evaluation and homing endonuclease activity.
Inteins are intervening sequences that are transcribed and translated with flanking host protein sequences and then self-excised by protein splicing. Bi-functional inteins also contain a homing endonuclease responsible for their genetic mobility. The PRP8 intein, the most widespread among fungi, occurs in important pathogens such as Histoplasma capsulatum and Paracoccidioides brasiliensis, from the Ajellomycetaceae family. Herein, we describe the bi-functional PRP8 intein in two other Ajellomycetacean pathogens, Blastomyces dermatitidis and Emmonsia parva. Sequence analysis and experimental evidence suggest that the homing endonuclease from PbrPRP8 is inactive. The splicing activity of the PRP8 intein from the B. dermatitidis, E. parva and P. brasiliensis species complex was demonstrated in a non-native protein context in Escherichia coli. Since the PRP8 intein is located in a functionally essential nuclear protein, it can be considered a promising therapeutic target for anti-fungal drugs, because inhibition of intein splicing should inhibit proliferation of intein-containing pathogens.
Ann file
T1 Species 460 482 Histoplasma capsulatum
N1 Reference T1 Taxonomy:5037
T2 Species 487 516 Paracoccidioides brasiliensis
N2 Reference T2 Taxonomy:121759
T3 Species 643 667 Blastomyces dermatitidis
N3 Reference T3 Taxonomy:5039
T4 Species 672 686 Emmonsia parva
N4 Reference T4 Taxonomy:73231
T5 Species 845 860 B. dermatitidis
N5 Reference T5 Taxonomy:5039
T6 Species 862 870 E. parva
N6 Reference T6 Taxonomy:73231
T7 Species 875 890 P. brasiliensis
N7 Reference T7 Taxonomy:121759
T8 Species 959 975 Escherichia coli
N8 Reference T8 Taxonomy:562