Molecular characterization of KEX1, a kexin-like protease in mouse Pneumocystis carinii.
Gene
; 242(1-2): 141-50, 2000 Jan 25.
Article
em En
| MEDLINE
| ID: mdl-10721706
ABSTRACT
Expression screening of a Pneumocystis carinii-infected mouse lung cDNA library with specific monoclonal antibodies (mAbs) led to the identification of a P. carinii cDNA with extensive homology to subtilisin-like proteases, particularly fungal kexins and mammalian prohormone convertases. The 3.1 kb cDNA contains a single open reading frame encoding 1011 amino acids. Structural similarities to fungal kexins in the deduced primary amino acid sequence include a putative proenzyme domain delineated by a consensus autocatalytic cleavage site (Arg-Glu-Lys-Arg), conserved Asp, His, Asn and Ser residues in the putative catalytic domain, a hydrophobic transmembrane spanning domain, and a carboxy-terminal cytoplasmic domain with a conserved tyrosine motif thought to be important for localization of the protease in the endoplasmic reticulum and/or Golgi apparatus. Based on these structural similarities and the classification of P. carinii as a fungus, the protease was named KEX1. Southern blotting of mouse P. carinii chromosomes localized kex1 to a single chromosome of approximately 610 kb. Southern blotting of restriction enzyme digests of genomic DNA from P. carinii-infected mouse lung demonstrated that kex1 is a single copy gene. The function of kexins in other fungi suggests that KEX1 may be involved in the post-translational processing and maturation of other P. carinii proteins.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pneumocystis
/
Carboxipeptidases
/
Subtilisinas
/
Proteínas de Saccharomyces cerevisiae
/
Pró-Proteína Convertases
Limite:
Animals
Idioma:
En
Revista:
Gene
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Estados Unidos