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The bornavirus-derived human protein EBLN1 promotes efficient cell cycle transit, microtubule organisation and genome stability. / Myers, Katie N; Barone, Giancarlo; Ganesh, Anil et al.
In: Scientific Reports, Vol. 6, 14.10.2016, p. 35548.

Research output: Contribution to journalArticlepeer-review

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Myers, KN, Barone, G, Ganesh, A, Staples, CJ, Howard, AE, Beveridge, RD, Maslen, S, Skehel, JM & Collis, SJ 2016, 'The bornavirus-derived human protein EBLN1 promotes efficient cell cycle transit, microtubule organisation and genome stability', Scientific Reports, vol. 6, pp. 35548. https://doi.org/10.1038/srep35548

APA

Myers, K. N., Barone, G., Ganesh, A., Staples, C. J., Howard, A. E., Beveridge, R. D., Maslen, S., Skehel, J. M., & Collis, S. J. (2016). The bornavirus-derived human protein EBLN1 promotes efficient cell cycle transit, microtubule organisation and genome stability. Scientific Reports, 6, 35548. https://doi.org/10.1038/srep35548

CBE

Myers KN, Barone G, Ganesh A, Staples CJ, Howard AE, Beveridge RD, Maslen S, Skehel JM, Collis SJ. 2016. The bornavirus-derived human protein EBLN1 promotes efficient cell cycle transit, microtubule organisation and genome stability. Scientific Reports. 6:35548. https://doi.org/10.1038/srep35548

MLA

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Myers KN, Barone G, Ganesh A, Staples CJ, Howard AE, Beveridge RD et al. The bornavirus-derived human protein EBLN1 promotes efficient cell cycle transit, microtubule organisation and genome stability. Scientific Reports. 2016 Oct 14;6:35548. doi: 10.1038/srep35548

Author

Myers, Katie N ; Barone, Giancarlo ; Ganesh, Anil et al. / The bornavirus-derived human protein EBLN1 promotes efficient cell cycle transit, microtubule organisation and genome stability. In: Scientific Reports. 2016 ; Vol. 6. pp. 35548.

RIS

TY - JOUR

T1 - The bornavirus-derived human protein EBLN1 promotes efficient cell cycle transit, microtubule organisation and genome stability

AU - Myers, Katie N

AU - Barone, Giancarlo

AU - Ganesh, Anil

AU - Staples, Christopher J

AU - Howard, Anna E

AU - Beveridge, Ryan D

AU - Maslen, Sarah

AU - Skehel, J Mark

AU - Collis, Spencer J

PY - 2016/10/14

Y1 - 2016/10/14

N2 - It was recently discovered that vertebrate genomes contain multiple endogenised nucleotide sequences derived from the non-retroviral RNA bornavirus. Strikingly, some of these elements have been evolutionary maintained as open reading frames in host genomes for over 40 million years, suggesting that some endogenised bornavirus-derived elements (EBL) might encode functional proteins. EBLN1 is one such element established through endogenisation of the bornavirus N gene (BDV N). Here, we functionally characterise human EBLN1 as a novel regulator of genome stability. Cells depleted of human EBLN1 accumulate DNA damage both under non-stressed conditions and following exogenously induced DNA damage. EBLN1-depleted cells also exhibit cell cycle abnormalities and defects in microtubule organisation as well as premature centrosome splitting, which we attribute in part, to improper localisation of the nuclear envelope protein TPR. Our data therefore reveal that human EBLN1 possesses important cellular functions within human cells, and suggest that other EBLs present within vertebrate genomes may also possess important cellular functions.

AB - It was recently discovered that vertebrate genomes contain multiple endogenised nucleotide sequences derived from the non-retroviral RNA bornavirus. Strikingly, some of these elements have been evolutionary maintained as open reading frames in host genomes for over 40 million years, suggesting that some endogenised bornavirus-derived elements (EBL) might encode functional proteins. EBLN1 is one such element established through endogenisation of the bornavirus N gene (BDV N). Here, we functionally characterise human EBLN1 as a novel regulator of genome stability. Cells depleted of human EBLN1 accumulate DNA damage both under non-stressed conditions and following exogenously induced DNA damage. EBLN1-depleted cells also exhibit cell cycle abnormalities and defects in microtubule organisation as well as premature centrosome splitting, which we attribute in part, to improper localisation of the nuclear envelope protein TPR. Our data therefore reveal that human EBLN1 possesses important cellular functions within human cells, and suggest that other EBLs present within vertebrate genomes may also possess important cellular functions.

U2 - 10.1038/srep35548

DO - 10.1038/srep35548

M3 - Article

C2 - 27739501

VL - 6

SP - 35548

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

ER -