دورية أكاديمية

Multiple cysteine proteinases of the pathogenic protozoon Tritrichomonas foetus: identification of seven diverse and differentially expressed genes.

التفاصيل البيبلوغرافية
العنوان: Multiple cysteine proteinases of the pathogenic protozoon Tritrichomonas foetus: identification of seven diverse and differentially expressed genes.
المؤلفون: Mallinson DJ; Department of Biological and Molecular Sciences, University of Stirling, UK., Livingstone J, Appleton KM, Lees SJ, Coombs GH, North MJ
المصدر: Microbiology (Reading, England) [Microbiology (Reading)] 1995 Dec; Vol. 141 ( Pt 12), pp. 3077-85.
نوع المنشور: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Microbiology Society Country of Publication: England NLM ID: 9430468 Publication Model: Print Cited Medium: Print ISSN: 1350-0872 (Print) Linking ISSN: 13500872 NLM ISO Abbreviation: Microbiology (Reading) Subsets: MEDLINE
أسماء مطبوعة: Publication: 2015- : London : Microbiology Society
Original Publication: Reading, U.K. : Society for General Microbiology, c1994-
مواضيع طبية MeSH: Genes, Protozoan*, Cysteine Endopeptidases/*genetics , Tritrichomonas foetus/*enzymology , Tritrichomonas foetus/*genetics, Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; Cloning, Molecular ; Cysteine Endopeptidases/isolation & purification ; DNA Primers/genetics ; DNA, Protozoan/genetics ; Gene Expression ; Genetic Variation ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; Sequence Homology, Amino Acid ; Species Specificity ; Tritrichomonas foetus/pathogenicity
مستخلص: The cattle protozoan parasite Tritrichomonas foetus has multiple forms of cysteine proteinases. To investigate their diversity, PCR and reverse transcriptase PCR were used to isolate genomic DNA and cDNA fragments, respectively, encoding different cysteine proteinases. Seven genes have been identified, TFCP3-6 from amplification of genomic DNA and TFCP7-9 from amplification of cDNA. Comparison of the predicted amino acid sequences indicates that the T. foetus enzymes are cathepsin-L-like rather than cathepsin-B-like in structure. However, there is considerable diversity among the proteinases. TFCP7 and TFCP8 are most similar to one another (78% identity), while TFCP3 and TFCP9 are the least closely related (30% identity). All but one of the genes are single-copy, the exception being TFCP3, which was present in multiple copies in one of the three isolates examined. Single transcripts were detected for each of the seven genes. TFCP8 was expressed at the highest levels, while transcripts for TFCP4 were only just detectable. In T. foetus F2, the strain from which the genomic DNA and mRNA were isolated, transcripts of the five other genes were present at intermediate levels. When two other isolates were compared with F2, differences in the expression of individual genes were apparent, with either one or two of them not expressed. In spite of these differences the major cysteine proteinases detected in the three isolates using substrate-SDS-PAGE appeared identical. The data show that the multiplicity of cysteine proteinases in T. foetus is due, in part at least, to the presence of multiple genes and that some of the genes encode cysteine proteinases which are not among the high-activity enzymes detected previously.
معلومات مُعتمدة: United Kingdom Wellcome Trust
سلسلة جزيئية: GENBANK U13153; U13154; X87776; X87777; X87778; X87779; X87780; X87781; X87782
المشرفين على المادة: 0 (DNA Primers)
0 (DNA, Protozoan)
EC 3.4.22.- (Cysteine Endopeptidases)
تواريخ الأحداث: Date Created: 19951201 Date Completed: 19960314 Latest Revision: 20200826
رمز التحديث: 20221213
DOI: 10.1099/13500872-141-12-3077
PMID: 8574401
قاعدة البيانات: MEDLINE
الوصف
تدمد:1350-0872
DOI:10.1099/13500872-141-12-3077