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Serine base‐exchange in rat liver nuclei
Author(s) -
Dygas Anna,
Przybyłek Krzysztof,
Meljon Anna,
Barańska Jolanta
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02058-5
Subject(s) - inner membrane , phosphatidylserine , serine , membrane , periplasmic space , biochemistry , chemistry , enzyme , organelle , trypsin , bacterial outer membrane , emerin , biophysics , biology , nuclear protein , phospholipid , escherichia coli , transcription factor , gene
It has been shown that the incorporation of [ 14 C]serine into phosphatidylserine (PS) in isolated rat liver nuclei is intrinsic to this organelle as attested by marker enzyme activity. Serine incorporation into PS was the highest in nuclei depleted of the outer membrane of the nuclear envelope (nucleoplasts) and negligible in the outer membrane. Trypsin treatment of nucleoplasts caused a strong inactivation of PS synthesis and only a moderate one of the NAD pyrophosphorylase activity, the marker enzyme of the inner nuclear membrane. We suggest that the serine base‐exchange enzyme is located in the inner membrane of the nuclear envelope and accessible from the periplasmic surface of this membrane.