NBP35 encodes an essential and evolutionary conserved protein in Saccharomyces cerevisiae with homology to a superfamily of bacterial ATPases
We have cloned a novel and essential gene, NBP35, from Saccharomyces cerevisiae that encodes a putative Nucleotide Binding Protein of 35 kDa. Sequence analysis revealed structural homology of Nbp35p with a family of bacterial ATPases involved in cell division processes and chromosome partitioning. A...
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| Main Authors: | , , |
|---|---|
| Format: | Article (Journal) |
| Language: | English |
| Published: |
1996
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| In: |
Gene
Year: 1996, Volume: 178, Issue: 1, Pages: 97-106 |
| ISSN: | 1879-0038 |
| DOI: | 10.1016/0378-1119(96)00341-1 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/0378-1119(96)00341-1 Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/0378111996003411 
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| Author Notes: | Gaetano Vitale, Emmanuelle Fabre, Eduard C. Hurt |
MARC
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| 520 | |a We have cloned a novel and essential gene, NBP35, from Saccharomyces cerevisiae that encodes a putative Nucleotide Binding Protein of 35 kDa. Sequence analysis revealed structural homology of Nbp35p with a family of bacterial ATPases involved in cell division processes and chromosome partitioning. A search in databases identified closely related sequences from yeast and higher eukaryotes, suggesting a conserved function for this family of proteins. By indirect immunofluorescence, a tagged version of Nbp35p carrying two immunoglobulin G-binding domains derived from Staphylococcus aureus Protein A was localised to the nucleus. A single amino-acid substitution in the conserved nucleotide-binding motif of Nbp35p renders the protein non-functional. Furthermore, a conserved cluster of four cysteines in the N-terminal end of the protein is also required for an essential role of Nbp35p. | ||
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