Evidence map›Paper›PMID 37645927›Full record

ArticlebioRxiv : the preprint server for biology2023

Site-specific acetylation of polynucleotide kinase 3'-phosphatase (PNKP) regulates its distinct role in DNA repair pathways.

Azharul Islam, Anirban Chakraborty, Altaf H Sarker, Uma K Aryal, Gulshan Sharma, Istvan Boldogh, Tapas Hazra

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Azharul IslamDepartment of Internal Medicine, University of Texas Medical Branch, Galveston, TX, 77555, USA.
Anirban ChakrabortyDepartment of Internal Medicine, University of Texas Medical Branch, Galveston, TX, 77555, USA.
Altaf H SarkerLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Uma K AryalPurdue Proteomics Facility, Bindley Bioscience Center, Purdue University, IN 47907, USA.
Gulshan SharmaDepartment of Internal Medicine, University of Texas Medical Branch, Galveston, TX, 77555, USA.
Istvan BoldoghDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Tapas HazraDepartment of Internal Medicine, University of Texas Medical Branch, Galveston, TX, 77555, USA.
The University of Texas Medical Branch at Galveston · USLawrence Berkeley National Laboratory · USPurdue University West Lafayette · US

Funding

Virus, Tissue Culture and ImmunoassayP01AI062885 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI GAROFALO, ROBERTO P · 2005 to 2022
$23.9M
Role of Cytosolic DNA-multiprotein Interactome in Allergic Airway InflammationR01HL145477 · NHLBI · UNIVERSITY OF TEXAS MED BR GALVESTON · PI HAZRA, TAPAS K, SUR, SANJIV · 2019 to 2022
$3.6M
Preferential single-strand break repair in the active genes of mammalian cellsR01NS073976 · NINDS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI HAZRA, TAPAS K · 2012 to 2021
$3.3M
NHLBI NIH HHS R01 HL145477NIAID NIH HHS P01 AI062885NINDS NIH HHS R01 NS073976
6 · The paper itself

Abstract

Mammalian polynucleotide kinase 3'-phosphatase (PNKP) is a dual-function DNA end-processing enzyme with 3'-phosphatase and 5'-kinase activities, which generate 3'-OH and 5'-phosphate termini respectively, as substrates for DNA polymerase and DNA ligase to complete DNA repair. PNKP is thus involved in multiple DNA repair pathways, including base excision (BER), single-strand break (SSBR), and double-strand break repair (DSBR). However, little is known as to how PNKP functions in such diverse repair processes, which involve distinct sets of proteins. In this study, we report that PNKP is acetylated at two lysine (K142 and K226) residues. While K142 (AcK142) is constitutively acetylated by p300, CBP acetylates K226 (AcK226) only after DSB induction. Co-immunoprecipitation analysis using antibodies specific for PNKP peptides containing AcK142 or AcK226 of PNKP showed that AcK142-PNKP associates only with BER/SSBR, and AcK226 PNKP only with DSBR proteins. Although acetylation at these residues did not significantly affect the enzymatic activity of PNKP

Identifiers

PMID37645927
PMCPMC10461918
OpenAlexW4381890714

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.