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A mechanism for memory storage insensitive to molecular turnover: a bistable autophosphorylating kinase.
Author(s) -
John Lisman
Publication year - 1985
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.9.3055
Subject(s) - bistability , autophosphorylation , mechanism (biology) , molecular switch , phosphorylation , microbiology and biotechnology , chemistry , kinase , biophysics , protein kinase a , biochemistry , materials science , biology , molecule , optoelectronics , physics , organic chemistry , quantum mechanics
A mechanism is proposed for a molecular switch that can store information indefinitely, despite the complete turnover of the molecules that make up the switch. The design of the switch is based on known types of biochemical reactions. Central to the mechanism is a kinase that is activated by phosphorylation and capable of intermolecular autophosphorylation. It is shown that such a kinase and an associated phosphatase form a bistable chemical switch that can be turned on by an external stimulus and that is not reset by protein turnover.

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