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Pregled bibliografske jedinice broj: 676260

Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo- glycohydrolase activities


Barkauskaite, Eva; Brassington, Amy; Tan, Edwin S.; Warwicker, Jim; Dunstan, Mark S.; Banos, Benito; Lafite, Pierre; Ahel, Marijan; Mitchison, Timothy J.; Ahel, Ivan; Leys, David
Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo- glycohydrolase activities // Nature communications, 4 (2013), 2164-1 doi:10.1038/ncomms3164 (međunarodna recenzija, članak, znanstveni)


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Naslov
Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo- glycohydrolase activities

Autori
Barkauskaite, Eva ; Brassington, Amy ; Tan, Edwin S. ; Warwicker, Jim ; Dunstan, Mark S. ; Banos, Benito ; Lafite, Pierre ; Ahel, Marijan ; Mitchison, Timothy J. ; Ahel, Ivan ; Leys, David

Izvornik
Nature communications (2041-1723) 4 (2013); 2164-1

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
glycosidase; poly(adenosine diphosphate ribose)

Sažetak
Poly-ADP-ribosylation is a post-translational modification that regulates processes involved in genome stability. Breakdown of the poly(ADP- ribose) (PAR) polymer is catalysed by poly(ADP- ribose) glycohydrolase (PARG), whose endo- glycohydrolase activity generates PAR fragments. Here we present the crystal structure of PARG incorporating the PAR substrate. The two terminal ADP-ribose units of the polymeric substrate are bound in exo-mode. Biochemical and modelling studies reveal that PARG acts predominantly as an exo- glycohydrolase. This preference is linked to Phe902 (human numbering), which is responsible for low-affinity binding of the substrate in endo-mode. Our data reveal the mechanism of poly- ADP-ribosylation reversal, with ADP- ribose as the dominant product, and suggest that the release of apoptotic PAR fragments occurs at unusual PAR/PARG ratios.

Izvorni jezik
Engleski

Znanstvena područja
Biologija



POVEZANOST RADA


Projekti:
098-0982934-2712 - Organski spojevi kao molekulski obilježivači antropogenog utjecaja na okoliš (Ahel, Marijan, MZOS ) ( POIROT)

Ustanove:
Institut "Ruđer Bošković", Zagreb

Profili:

Avatar Url Marijan Ahel (autor)

Avatar Url Ivan Ahel (autor)

Poveznice na cjeloviti tekst rada:

doi fulir.irb.hr www.nature.com

Citiraj ovu publikaciju:

Barkauskaite, Eva; Brassington, Amy; Tan, Edwin S.; Warwicker, Jim; Dunstan, Mark S.; Banos, Benito; Lafite, Pierre; Ahel, Marijan; Mitchison, Timothy J.; Ahel, Ivan; Leys, David
Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo- glycohydrolase activities // Nature communications, 4 (2013), 2164-1 doi:10.1038/ncomms3164 (međunarodna recenzija, članak, znanstveni)
Barkauskaite, E., Brassington, A., Tan, E., Warwicker, J., Dunstan, M., Banos, B., Lafite, P., Ahel, M., Mitchison, T., Ahel, I. & Leys, D. (2013) Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo- glycohydrolase activities. Nature communications, 4, 2164-1 doi:10.1038/ncomms3164.
@article{article, author = {Barkauskaite, Eva and Brassington, Amy and Tan, Edwin S. and Warwicker, Jim and Dunstan, Mark S. and Banos, Benito and Lafite, Pierre and Ahel, Marijan and Mitchison, Timothy J. and Ahel, Ivan and Leys, David}, year = {2013}, pages = {2164-1-2164-8}, DOI = {10.1038/ncomms3164}, keywords = {glycosidase, poly(adenosine diphosphate ribose)}, journal = {Nature communications}, doi = {10.1038/ncomms3164}, volume = {4}, issn = {2041-1723}, title = {Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo- glycohydrolase activities}, keyword = {glycosidase, poly(adenosine diphosphate ribose)} }
@article{article, author = {Barkauskaite, Eva and Brassington, Amy and Tan, Edwin S. and Warwicker, Jim and Dunstan, Mark S. and Banos, Benito and Lafite, Pierre and Ahel, Marijan and Mitchison, Timothy J. and Ahel, Ivan and Leys, David}, year = {2013}, pages = {2164-1-2164-8}, DOI = {10.1038/ncomms3164}, keywords = {glycosidase, poly(adenosine diphosphate ribose)}, journal = {Nature communications}, doi = {10.1038/ncomms3164}, volume = {4}, issn = {2041-1723}, title = {Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo- glycohydrolase activities}, keyword = {glycosidase, poly(adenosine diphosphate ribose)} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


Citati:





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