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Background  The gene  YCL047C , which has been renamed promoter of filamentation gene ( POF1 ), has recently been described as a cell component involved in yeast filamentous growth. The objective of this work is to understand the molecular and biological function of this gene.    Results  Here, we report that the protein encoded by the  POF1  gene, Pof1p, is an ATPase that may be part of the  Saccharomyces cerevisiae  protein quality control pathway. According to the results,  Δpof1  cells showed increased sensitivity to hydrogen peroxide,  tert -butyl hydroperoxide, heat shock and protein unfolding agents, such as dithiothreitol and tunicamycin. Besides, the overexpression of  POF1  suppressed the sensitivity of  Δpct1 , a strain that lacks a gene that encodes a phosphocholine cytidylyltransferase, to heat shock.  In vitro  analysis showed, however, that the purified Pof1p enzyme had no cytidylyltransferase activity but does have ATPase activity, with catalytic efficiency comparable to other ATPases involved in endoplasmic reticulum-associated degradation of proteins (ERAD). Supporting these findings,  co-immunoprecipitation  experiments showed a physical interaction between Pof1p and Ubc7p (an ubiquitin conjugating enzyme)  in vivo .    Conclusions  Taken together, the results strongly suggest that the biological function of Pof1p is related to the regulation of protein degradation.

The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process