منابع مشابه
Yeast-based genetic system for functional analysis of poxvirus mRNA cap methyltransferase.
Structural differences between poxvirus and human mRNA capping enzymes recommend cap formation as a target for antipoxviral drug discovery. Genetic and pharmacologic analysis of the poxvirus capping enzymes requires in vivo assays in which the readout depends on the capacity of the viral enzyme to catalyze cap synthesis. Here we have used the budding yeast Saccharomyces cerevisiae as a genetic ...
متن کاملmRNA Cap-1 Methyltransferase in the SARS Genome
The 3D jury system has predicted the methyltransferase fold for the nsp13 protein of the SARS coronavirus. Based on the conservation of a characteristic tetrad of residues, the mRNA cap-1 methyltransferase function has been assigned to this protein, which has potential implications for antiviral therapy.
متن کاملThe Candida albicans gene for mRNA 5-cap methyltransferase: identification of additional residues essential for catalysis.
The 5'-cap structure of eukaryotic mRNA is methylated at the terminal guanosine by RNA (guanine-N7-)-methyltransferase (cap MTase). Saccharomyces cerevisiae ABD1 (ScABD1) and human hMet (also called CMT1) genes are responsible for this enzyme. The ABD1 homologue was cloned from the pathogenic fungus Candida albicans and named C. albicans ABD1 (CaABD1). When expressed as a fusion with glutathion...
متن کاملRegulation of mRNA cap methylation
The 7-methylguanosine cap added to the 5' end of mRNA is essential for efficient gene expression and cell viability. Methylation of the guanosine cap is necessary for the translation of most cellular mRNAs in all eukaryotic organisms in which it has been investigated. In some experimental systems, cap methylation has also been demonstrated to promote transcription, splicing, polyadenylation and...
متن کاملCap-dependent deadenylation of mRNA.
Poly(A) tail removal is often the initial and rate-limiting step in mRNA decay and is also responsible for translational silencing of maternal mRNAs during oocyte maturation and early development. Here we report that deadenylation in HeLa cell extracts and by a purified mammalian poly(A)-specific exoribonuclease, PARN (previously designated deadenylating nuclease, DAN), is stimulated by the pre...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2006
ISSN: 0021-9258
DOI: 10.1074/jbc.m602867200