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Muscle FBPase is targeted to nucleus by its 203 KKKGK 207 sequence
Author(s) -
Gizak Agnieszka,
MaciaszczykDziubinska Ewa,
Jurowicz Magdalena,
Rakus Dariusz
Publication year - 2009
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22506
Subject(s) - nls , nuclear localization sequence , fructose 1,6 bisphosphatase , nuclear transport , in silico , transfection , biology , enzyme , nucleus , microbiology and biotechnology , biochemistry , cell nucleus , gene
It has been recently found that muscle fructose 1,6‐bisphosphatase (FBPase) is actively transported into cells' nuclei. Results of an analysis in silico of muscle FBPase structure gave rise to a hypothesis that sequence 203 KKKGK 207 is responsible for nuclear targeting of the enzyme. To test this, HL‐1 cardiomyocytes were transfected with FITC‐labeled muscle FBPase constructs, bearing mutations within the putative nuclear localization signal (NLS). Results revealed that integrity of the 203 KKKGK 207 motif is critical to nuclear targeting of muscle FBPase and even a single amino‐acid change within this sequence results in significant decrease of nuclear accumulation of the enzyme. Although it has long been recognized as a canonical NLS in theoretical and computational research, to the best of our knowledge this is the first experimental evidence confirming that the KKKGK motif can act as a functional NLS in a protein. Proteins 2009. © 2009 Wiley‐Liss, Inc.