Basic amino acid residues located in the N-terminal region of BEND3 are essential for its nuclear localization

Hirokazu Shiheido; Jun Shimizu

doi:10.1016/j.bbrc.2015.01.029

Basic amino acid residues located in the N-terminal region of BEND3 are essential for its nuclear localization

Biochem Biophys Res Commun. 2015 Feb 20;457(4):589-94. doi: 10.1016/j.bbrc.2015.01.029. Epub 2015 Jan 16.

Authors

Hirokazu Shiheido¹, Jun Shimizu²

Affiliations

¹ Center for Innovation in Immunoregulative Technology and Therapeutics, Graduate School of Medicine, Kyoto University, Kyoto, Japan. Electronic address: shiheido@ak.med.kyoto-u.ac.jp.
² Center for Innovation in Immunoregulative Technology and Therapeutics, Graduate School of Medicine, Kyoto University, Kyoto, Japan.

PMID: 25600804
DOI: 10.1016/j.bbrc.2015.01.029

Abstract

BEN domain-containing protein 3 (BEND3) has recently been reported to function as a heterochromatin-associated protein in transcriptional repression in the nucleus. BEND3 should have nuclear localization signals (NLSs) to localize to the nucleus in light of its molecular weight, which is higher than that allowed to pass through nuclear pore complexes. We here analyzed the subcellular localization of deletion/site-directed mutants of human BEND3 by an immunofluorescence assay in an attempt to identify the amino acids essential for its nuclear localization. We found that three basic amino acid residues located in the N-terminal region of BEND3 (BEND356-58, KRK) are essential, suggesting that these residues play a role as a functional NLS. These results provide valuable information for progressing research on BEND3.

Keywords: BEND3; HeLa; NLS.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Amino Acids, Basic / analysis*
Cell Nucleus / chemistry*
HeLa Cells
Humans
Molecular Sequence Data
Nuclear Localization Signals
Repressor Proteins / analysis*

Substances

Amino Acids, Basic
BEND3 protein, human
Nuclear Localization Signals
Repressor Proteins