**1. PARP Family and Structure:**
– PARP family consists of 17 members (10 putative) with varying structures and functions.
– PARP1, PARP2, VPARP (PARP4), Tankyrase-1, and -2 exhibit confirmed PARP activity.
– Comprised of DNA-binding, caspase-cleaved, auto-modification, and catalytic domains.
– DNA-binding domain contains zinc finger motifs and is involved in programmed cell death.
**2. Functions of PARP:**
– Detects and responds to single-strand DNA breaks.
– Initiates repair by synthesizing poly (ADP-ribose) chains using NAD+.
– Regulates basal bioenergetics and expression of inflammatory genes.
**3. Role in DNA Repair:**
– Assists in repairing single-strand DNA nicks through base excision repair.
– PARP-1 and PARP-2 are activated by DNA single-strand breaks.
– Tankyrases interact with telomere-associated proteins and play roles in vesicular trafficking and mitotic spindle assembly.
**4. Therapeutic Applications and Inhibition:**
– PARP inhibitors are effective in various cancers, especially in HRR-defective cancers.
– Biomarkers are needed to identify HRR defects for broader use of PARP inhibitors.
– Inactivation by caspase cleavage leads to programmed cell death and prevents repair at damaged sites.
**5. Plant PARPs and Additional Information:**
– Plant PARPs respond to DNA damage and stress, with PARP1 and PARP2 playing crucial roles.
– PARP2 in plants has different domains and is significant in protective responses.
– Research studies explore the role of PARP in DNA repair, genomic integrity, cell death, and aging.
– Therapeutic applications beyond cancer treatment and repurposing of PARP inhibitors are being investigated.
Poly (ADP-ribose) polymerase (PARP) is a family of proteins involved in a number of cellular processes such as DNA repair, genomic stability, and programmed cell death.
poly [ADP-ribose] polymerase | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
Aliases | Poly (ADP-ribose) polymerasePARPNAD+ ADP-ribosyltransferaseIPR008288poly(adenosine diphosphate ribose) polymerasepoly(ADP-ribose) synthasepoly(ADP-ribose) synthetaseNAD+:poly(adenine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyl-transferaseADP-ribosyltransferase (polymerizing)Poly(ADP-ribose) Polymerases | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | GeneCards: [1] | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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NAD+ ADP-ribosyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.4.2.30 | ||||||||
CAS no. | 58319-92-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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