NDLI: Characterization of Candida albicans RNA triphosphatase and mutational analysis of its active site

Content Provider	PubMed Central
Author	Pei, Yi Lehman, Kevin Tian, Ligeng Shuman, Stewart
Copyright Year	2000
Abstract	The RNA triphosphatase component (CaCet1p) of the mRNA capping apparatus of the pathogenic fungus Candida albicans differs mechanistically and structurally from the RNA triphosphatase of mammals. Hence, CaCet1p is an attractive antifungal target. Here we identify a C-terminal catalytic domain of CaCet1p from residue 257 to 520 and characterize a manganese-dependent and cobalt-dependent NTPase activity intrinsic to CaCet1p. The NTPase can be exploited to screen in vitro for inhibitors. The amino acids that comprise the active site of CaCet1p were identified by alanine-scanning mutagenesis, which was guided by the crystal structure of the homologous RNA triphosphatase from Saccharomyces cerevisiae (Cet1p). Thirteen residues required for the phosphohydrolase activity of CaCet1p (Glu287, Glu289, Asp363, Arg379, Lys396, Glu420, Arg441, Lys443, Arg445, Asp458, Glu472, Glu474 and Glu476) are located within the hydrophilic interior of an eight-strand β barrel of Cet1p. Each of the eight strands contributes at least one essential amino acid. The essential CaCet1p residues include all of the side chains that coordinate manganese and sulfate (i.e., γ phosphate) in the Cet1p product complex. These results suggest that the active site structure and catalytic mechanism are conserved among fungal RNA triphosphatases.
Starting Page	1885
File Format	PDF
ISSN	13624962
e-ISSN	13624962
Journal	Nucleic Acids Research
Issue Number	9
Volume Number	28
Language	English
Publisher	Oxford University Press
Publisher Date	2000-05-01
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Genetics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Characterization and mutational analysis of the transcription factor Acpr cphj in Candida Albicans

RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans

An active retrotransposon in Candida albicans

Mutational Analysis of Candida albicans SNF7 Reveals Genetically Separable Rim101 and ESCRT Functions and Demonstrates Divergence in bro1-Domain Protein Interactions

Site-directed mutational analysis of the novel catalytic domains of α-aminoadipate reductase (Lys2p) from Candida albicans

RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans

Characterization of Schizosaccharomyces pombe RNA triphosphatase

Identification and characterization of TUP1-regulated genes in Candida albicans.

Mutational analysis of the RNA triphosphatase component of vaccinia virus mRNA capping enzyme.

Characterization of Candida albicans RNA triphosphatase and mutational analysis of its active site

Similar Documents

Characterization and mutational analysis of the transcription factor Acpr cphj in Candida Albicans

RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans

An active retrotransposon in Candida albicans

Mutational Analysis of Candida albicans SNF7 Reveals Genetically Separable Rim101 and ESCRT Functions and Demonstrates Divergence in bro1-Domain Protein Interactions

Site-directed mutational analysis of the novel catalytic domains of α-aminoadipate reductase (Lys2p) from Candida albicans

RNA triphosphatase is essential in Schizosaccharomyces pombe and Candida albicans

Characterization of Schizosaccharomyces pombe RNA triphosphatase

Identification and characterization of TUP1-regulated genes in Candida albicans.

Mutational analysis of the RNA triphosphatase component of vaccinia virus mRNA capping enzyme.

Characterization of Candida albicans RNA triphosphatase and mutational analysis of its active site