Karwan, R MLaroche, TWintersberger, UGasser, S MBinder, M2009-02-192009-02-192009-02-191990https://infoscience.epfl.ch/handle/20.500.14299/35563We have used monospecific antibodies against three ribonuclease H enzymes of Saccharomyces cerevisiae to investigate their intracellular localization. Fractionation experiments, as well as immunocytochemical staining, revealed a predominantly cytoplasmic localization of the RNase H proteins of 42,000 and 70,000 Mr, whereas that of 55,000 Mr showed equal distribution between nuclei and cytoplasm. The nuclear moiety of ribonuclease H(70) was found to be a part of the yeast nuclear scaffold, as investigated by immunoblotting and antibody inhibition experiments. The 42,000 and 55,000 Mr enzymes, on the other hand, are not scaffold-associated. We conclude that RNase H(70) is part of the nuclear substructure of yeast that was previously found to maintain specific interactions with yeast chromosomal origins of replication (ARS elements).text::journal::journal article::research article