Molecular Insights into Poly(ADP-ribose) Recognition and Processing
Poly(ADP-ribosyl)ation is a post-translational protein modification involved in the regulation of important cellular functions including DNA repair, transcription, mitosis and apoptosis. The amount of poly(ADP-ribosyl)ation (PAR) in cells reflects the balance of synthesis, mediated by the PARP prote...
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Online Access: | http://www.mdpi.com/2218-273X/3/1/1 |
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doaj-8f84410a620e4e40a78c734cd3209b702020-11-24T23:06:40ZengMDPI AGBiomolecules2218-273X2012-12-013111710.3390/biom3010001Molecular Insights into Poly(ADP-ribose) Recognition and ProcessingIvan AhelEva BarkauskaiteRoko ŽajaAndreja MikočPoly(ADP-ribosyl)ation is a post-translational protein modification involved in the regulation of important cellular functions including DNA repair, transcription, mitosis and apoptosis. The amount of poly(ADP-ribosyl)ation (PAR) in cells reflects the balance of synthesis, mediated by the PARP protein family, and degradation, which is catalyzed by a glycohydrolase, PARG. Many of the proteins mediating PAR metabolism possess specialised high affinity PAR-binding modules that allow the efficient sensing or processing of the PAR signal. The identification of four such PAR-binding modules and the characterization of a number of proteins utilising these elements during the last decade has provided important insights into how PAR regulates different cellular activities. The macrodomain represents a unique PAR-binding module which is, in some instances, known to possess enzymatic activity on ADP-ribose derivatives (in addition to PAR-binding). The most recently discovered example for this is the PARG protein, and several available PARG structures have provided an understanding into how the PARG macrodomain evolved into a major enzyme that maintains PAR homeostasis in living cells.http://www.mdpi.com/2218-273X/3/1/1Poly(ADP-ribose)PARPPARGmacrodomainprotein modification |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ivan Ahel Eva Barkauskaite Roko Žaja Andreja Mikoč |
spellingShingle |
Ivan Ahel Eva Barkauskaite Roko Žaja Andreja Mikoč Molecular Insights into Poly(ADP-ribose) Recognition and Processing Biomolecules Poly(ADP-ribose) PARP PARG macrodomain protein modification |
author_facet |
Ivan Ahel Eva Barkauskaite Roko Žaja Andreja Mikoč |
author_sort |
Ivan Ahel |
title |
Molecular Insights into Poly(ADP-ribose) Recognition and Processing |
title_short |
Molecular Insights into Poly(ADP-ribose) Recognition and Processing |
title_full |
Molecular Insights into Poly(ADP-ribose) Recognition and Processing |
title_fullStr |
Molecular Insights into Poly(ADP-ribose) Recognition and Processing |
title_full_unstemmed |
Molecular Insights into Poly(ADP-ribose) Recognition and Processing |
title_sort |
molecular insights into poly(adp-ribose) recognition and processing |
publisher |
MDPI AG |
series |
Biomolecules |
issn |
2218-273X |
publishDate |
2012-12-01 |
description |
Poly(ADP-ribosyl)ation is a post-translational protein modification involved in the regulation of important cellular functions including DNA repair, transcription, mitosis and apoptosis. The amount of poly(ADP-ribosyl)ation (PAR) in cells reflects the balance of synthesis, mediated by the PARP protein family, and degradation, which is catalyzed by a glycohydrolase, PARG. Many of the proteins mediating PAR metabolism possess specialised high affinity PAR-binding modules that allow the efficient sensing or processing of the PAR signal. The identification of four such PAR-binding modules and the characterization of a number of proteins utilising these elements during the last decade has provided important insights into how PAR regulates different cellular activities. The macrodomain represents a unique PAR-binding module which is, in some instances, known to possess enzymatic activity on ADP-ribose derivatives (in addition to PAR-binding). The most recently discovered example for this is the PARG protein, and several available PARG structures have provided an understanding into how the PARG macrodomain evolved into a major enzyme that maintains PAR homeostasis in living cells. |
topic |
Poly(ADP-ribose) PARP PARG macrodomain protein modification |
url |
http://www.mdpi.com/2218-273X/3/1/1 |
work_keys_str_mv |
AT ivanahel molecularinsightsintopolyadpriboserecognitionandprocessing AT evabarkauskaite molecularinsightsintopolyadpriboserecognitionandprocessing AT rokozaja molecularinsightsintopolyadpriboserecognitionandprocessing AT andrejamikoc molecularinsightsintopolyadpriboserecognitionandprocessing |
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