Cover Image

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...

Full description

Saved in:
Bibliographic Details
Main Authors: Vitale, Gaetano (Author) , Fabre, Emmanuelle (Author) , Hurt, Ed (Author)
Format: Article (Journal)
Language:English
Published: 1996
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
Get full text
Author Notes:Gaetano Vitale, Emmanuelle Fabre, Eduard C. Hurt
Description
Summary: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.
Item Description:Elektronische Reproduktion der Druck-Ausgabe 22. März 1999
Gesehen am 29.01.2026
Physical Description:Online Resource
ISSN:1879-0038
DOI:10.1016/0378-1119(96)00341-1

Similar Items