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The essential function of Swc4p - a protein shared by two chromatin-modifying complexes of the yeast Saccharomyces cerevisiae - resides within its N-terminal part

100%
Miciałkiewicz A., Chełstowska A.
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2008
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vol. 55
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issue 3
603-612
EN
The Swc4p protein, encoded by an essential gene, is shared by two chromatin-remodeling complexes in Saccharomyces cerevisiae cells: NuA4 (nucleosome acetyltransferase of H4) and SWR1. The SWR1 complex catalyzes ATP-dependent exchange of the nucleosomal histone H2A for H2AZ (Htz1p). The activity of NuA4 is responsible mainly for the acetylation of the H4 histone but also for the acetylation of H2A and H2AZ. In this work we investigated the role of the Swc4p protein. Using random mutagenesis we isolated a collection of swc4 mutants and showed that the essential function of Swc4p resides in its N-terminal part, within the first 269 amino acids of the 476-amino acid-long protein. We also demonstrated that Swc4p is able to accommodate numerous mutations without losing its functionality under standard growth conditions. However, when swc4 mutants were exposed to methyl methanesulfonate (MMS), hydroxyurea or benomyl, severe growth deficiencies appeared, pointing to an involvement of Swc4p in many chromatin-based processes. The mutants' phenotypes did not result from an impairment of histone acetylation, as in the mutant which bears the shortest isolated variant of truncated Swc4p, the level of overall H4 acetylation was unchanged.
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YOR129c, a new element interacting with Cnm67p, a component of the spindle pole body of Saccharomyces cerevisiae.

81%
Wysocka M., Białkowska A., Miciałkiewicz A., Kurlandzka A.
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2003
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vol. 50
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issue 3
883-890
EN
The Saccharomyces cerevisiae spindle pole body (SPB) consists of numerous proteins forming the outer, inner and central plaques. The protein Cnm67 is an important component of the outer plaque. The C-terminus of this protein contains a determinant important for its SPB localization. We identified a protein encoded by YOR129c which interacts with this C-terminus in the two-hybrid system. YOR129c and CNM67 exhibit weak genetic interaction. The double deletion strain yor129cΔ cnm67Δ exhibits moderately increased resistance to 0.1 M LiCl and hygromycin B compared with the cnm67Δ single mutant. We propose that the YOR129c protein is an accessory factor associated with the cytoplasmic face of SPB and plays a role in cation homeostasis and/or multidrug resistance.
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