Document Detail

Role of N-terminal hydrophobic region in modulating the subcellular localization and enzyme activity of the bisphosphate nucleotidase from Debaryomyces hansenii.
MedLine Citation:
PMID:  16467467     Owner:  NLM     Status:  MEDLINE    
3', 5'-Bisphosphate nucleotidase is a ubiquitous enzyme that converts 3'-phosphoadenosine-5'-phosphate to adenosine-5'-phosphate and inorganic phosphate. These enzymes are highly sensitive to sodium and lithium and, thus, perform a crucial rate-limiting metabolic step during salt stress in yeast. Recently, we have identified a bisphosphate nucleotidase gene (DHAL2) from the halotolerant yeast Debaryomyces hansenii. One of the unique features of Dhal2p is that it contains an N-terminal 54-amino-acid-residue hydrophobic extension. In this study, we have shown that Dhal2p exists as a cytosolic as well as a membrane-bound form and that salt stress markedly influences the accumulation of the latter form in the cell. We have demonstrated that the N-terminal hydrophobic region was necessary for the synthesis of the membrane-bound isoform. It appeared that an alternative translation initiation was the major mechanism for the synthesis of these two forms. Moreover, the two forms exhibit significant differences in their substrate specificity. Unlike the cytosolic form, the membrane-bound form showed very high activity against inositol-1,4-bisphosphate. Thus, the present study for the first time reports the existence of multiple forms of a bisphosphate nucleotidase in any organism.
Monika Aggarwal; Alok K Mondal
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Eukaryotic cell     Volume:  5     ISSN:  1535-9778     ISO Abbreviation:  Eukaryotic Cell     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-02-09     Completed Date:  2006-05-08     Revised Date:  2013-06-07    
Medline Journal Info:
Nlm Unique ID:  101130731     Medline TA:  Eukaryot Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  262-71     Citation Subset:  IM    
Institute of Microbial Technology, Sector 39A, Chandigarh 160 036, India.
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MeSH Terms
Amino Acid Sequence
Codon, Initiator / genetics
Gene Expression Profiling
Genes, Fungal / genetics
Genetic Vectors
Hydrophobic and Hydrophilic Interactions*
Membranes / metabolism
Molecular Sequence Data
Mutation / genetics
Nucleotidases / chemistry*,  metabolism*
Peptide Chain Initiation, Translational / genetics
Phosphoric Monoester Hydrolases / metabolism
Protein Transport
Saccharomycetales / cytology*,  enzymology*,  growth & development
Salts / metabolism
Reg. No./Substance:
0/Codon, Initiator; 0/Salts; EC 3.1.3.-/Nucleotidases; EC 3.1.3.-/Phosphoric Monoester Hydrolases; EC,4-bisphosphate 1-phosphatase; EC 3'-nucleotidase

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