Motifs in the amino-terminus of CENP-A are required for its accumulation within the nucleus and at the centromere
PDF | HTML | How to cite
Metrics: PDF 1678 views | HTML 1881 views | ?
Ruiqi Jing1, Jiajie Xi1, Ye Leng1, Wen Chen1, Guiying Wang1, Wenwen Jia1, Jiuhong Kang1 and Songcheng Zhu1
1Clinical and Translational Research Center of Shanghai First Maternity and Infant Health Hospital, Shanghai Key Laboratory of Signaling and Disease Research, Collaborative Innovation Center for Brain Science, School of Life Science and Technology, Tongji University, Shanghai, 200092, China
Songcheng Zhu, email: [email protected]
Jiuhong Kang, email: [email protected]
Keywords: centromeric protein A (CENP-A), histone variant, nuclear localization, centromeric localization
Received: January 04, 2017 Accepted: April 07, 2017 Published: April 18, 2017
Centromere protein A (CENP-A) is a variant of core histone H3 that marks the centromere’s location on the chromosome. The mechanisms that target the protein to the nucleus and the centromere have not been defined. In this study, we found that deletion of the first 53 but not the first 29 residues of CENP-A from the amino-terminus, resulted in its cytoplasmic localization. Two motifs, R42R43R44 and K49R52K53K56, which are reported to be required for DNA contact in the centromere nucleosome, were found to be critical for CENP-A nuclear accumulation. These two motifs potentially mediated its interaction with Importin-β but were not involved in CENP-A centromeric localization. A third novel motif, L60L61I62R63K64, was found to be essential for the centromeric accumulation of CENP-A. The nonpolar hydrophobic residues L60L61I62, but not the basic residues R63K64, were found to be the most important residues. A protein interaction assay suggested that this motif is not involved in the interaction of CENP-A with its deposition factors but potentially mediates its interaction with core histone H4 and CENP-B. Our study uncovered the role of the amino-terminus of CENP-A in localization.
All site content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 License.