Cleavage efficiency by adenovirus protease is site-dependent.

The Journal of Biological Chemistry
M DiouriJ M Weber

Abstract

The adenovirus protease cleaves consensus sequences (M/I/L)XGX-G and (M/I/L)XGG-X. Using purified recombinant protease, we showed that a peptide bearing the GX-G site was hydrolyzed more rapidly than a peptide bearing the GG-X site. The GX-G site was also preferentially cleaved on viral protein pVI which bears both sites of cleavage. Evidence is presented that suggests a biological role for this differential cleavage efficiency.

References

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Citations

Oct 9, 2002·Virus Research·Angelique Ruzindana-UmunyanaJoseph M Weber
Nov 26, 2014·Viruses·Walter F Mangel, Carmen San Martín
Mar 13, 2014·Journal of Molecular Biology·Joost SnijderAlbert J R Heck
Apr 19, 2011·International Journal of Mass Spectrometry·Catherine FenselauStephen Swatkoski
Jul 1, 2009·Journal of Molecular Biology·Ana J Pérez-BernáCarmen San Martín
Sep 13, 2008·Journal of Molecular Biology·Carmen San MartínIgor P Dmitriev
Feb 8, 2014·Virology·Lingpeng ChengPing Zhu
Jun 10, 2003·Acta Microbiologica Et Immunologica Hungarica·Joseph M Weber
Nov 12, 2013·Virology·Sara Bergström LindUlf Pettersson
Mar 17, 2017·Journal of Virology·Amit GabaSuresh Tikoo
Nov 30, 2019·FEBS Letters·Glen Nemerow, Jane Flint
Jul 4, 2012·Viruses·Carmen San Martín
Mar 7, 2021·Viruses·Shermila Kulanayake, Suresh K Tikoo

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