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The Long Linker Region of Telomere-Binding Protein TRF2 Is Responsible for Interactions with Lamins by Aleksandra O. Travina; Nadya V. Ilicheva; Alexey G. Mittenberg; Sergey V. Shabelnikov; Anastasia V. Kotova; Olga I. Podgornaya is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Telomere-binding factor 2 (TRF2) is part of the shelterin protein complex found at chromosome ends. Lamin A/C interacts with TRF2 and influences telomere position. TRF2 has an intrinsically disordered region between the ordered dimerization and DNA-binding domains. This domain is referred to as the long linker region of TRF2, or udTRF2. We suggest that udTRF2 might be involved in the interaction between TRF2 and lamins. The recombinant protein corresponding to the udTRF2 region along with polyclonal antibodies against this region were used in co-immunoprecipitation with purified lamina and nuclear extracts. Co-immunoprecipitation followed by Western blots and mass spectrometry indicated that udTRF2 interacts with lamins, preferably lamins A/C. The interaction did not involve any lamin-associated proteins, was not dependent on the post-translation modification of lamins, nor did it require their higher-order assembly. Besides lamins, a number of other udTRF2-interacting proteins were identified by mass spectrometry, including several heterogeneous nuclear ribonucleoproteins (hnRNP A2/B1, hnRNPA1, hnRNP A3, hnRNP K, hnRNP L, hnRNP M), splicing factors (SFPQ, NONO, SRSF1, and others),

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Author

Aleksandra O. Travina; Nadya V. Ilicheva; Alexey G. Mittenberg; Sergey V. Shabelnikov; Anastasia V. Kotova; Olga I. Podgornaya

Publisher

MDPI AG

Published

2021

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)