Document Detail


Two domains with amino-acid sequence similarity are required for dihydroneopterin aldolase function in the multifunctional folic acid synthesis Fas protein of Pneumocystis carinii.
MedLine Citation:
PMID:  7543066     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The folic acid synthesized gene (fas) of Pneumocystis carinii (Pc) codes for a multifunctional enzyme (Fas) known to catalyse three consecutive steps leading to the production of dihydropteroate in the de novo folate synthesis pathway. Previously, we predicted that a domain, designated FasB (amino acids (aa) 161-280), of the 740-aa multifunctional protein contains the first of the three enzyme activities in the pathway, namely dihydroneopterin aldolase (DHNA), since it shares 23% aa identity with the DHNA of Streptococcus pneumoniae (Sp). We now extend these findings to show that a second domain, FasA (aa 39-160), whose function was previously unknown, shares 27% sequence identity with the adjacent FasB domain, indicative of functional similarity. FasA is also 18% identical with the DHNA from Sp. Recombinant baculoviruses were constructed which directed the production of either FasA, FasB or FasAB polypeptide species in cultured Spodoptera frugiperda (SF9) insect cells. No DHNA activity is associated with either fasA or fasB when produced as single domains in the insect-baculovirus system. However, DHNA activity was detected in SF9 extracts containing the overproduced FasAB polypeptide. The results of aa sequence alignments and expression studies suggest that FasA and FasB may be two subunits of the DHNA enzyme moiety within the multifunctional Fas protein of Pc. An alternative interpretation of the results is also discussed.
Authors:
F Volpe; S P Ballantine; C J Delves
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Gene     Volume:  160     ISSN:  0378-1119     ISO Abbreviation:  Gene     Publication Date:  1995 Jul 
Date Detail:
Created Date:  1995-09-07     Completed Date:  1995-09-07     Revised Date:  2009-09-29    
Medline Journal Info:
Nlm Unique ID:  7706761     Medline TA:  Gene     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  41-6     Citation Subset:  IM    
Affiliation:
Structural Biology Group, Wellcome Research Laboratories, Beckenham, Kent, UK.
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MeSH Terms
Descriptor/Qualifier:
Aldehyde-Lyases / genetics,  metabolism*
Amino Acid Sequence
Animals
Antigens, CD95
Antigens, Surface / genetics,  metabolism*
Base Sequence
Blotting, Western
Cell Line
DNA Primers
Folic Acid / biosynthesis
Fungal Proteins / genetics,  metabolism*
Genes, Fungal
Kinetics
Molecular Sequence Data
Open Reading Frames
Pneumocystis / enzymology*,  genetics
Recombinant Proteins / metabolism
Sequence Homology, Amino Acid
Spodoptera
Streptococcus pneumoniae / genetics
Transfection
Grant Support
ID/Acronym/Agency:
//Wellcome Trust
Chemical
Reg. No./Substance:
0/Antigens, CD95; 0/Antigens, Surface; 0/DNA Primers; 0/FasA protein, Pneumocystis; 0/FasB protein, Pneumocystis; 0/Fungal Proteins; 0/Recombinant Proteins; 59-30-3/Folic Acid; EC 4.1.2.-/Aldehyde-Lyases; EC 4.1.2.25/dihydroneopterin aldolase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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