Evidence map›Paper›PMID 39826527›Full record

ArticleBiochemical and biophysical research communications2025

Structural, functional, and regulatory evaluation of a cysteine post-translationally modified Gcn5-related N-acetyltransferase.

Patricia Uychoco, Karolina A Majorek, Ashley N Ives, Van Thi Bich Le, Pamela L Caro De Silva, Vanessa L Paurus, Isaac Kwame Attah, Mary S Lipton, Wladek Minor, Misty L Kuhn

Abstract read
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In one paragraph

Article in Biochemical and biophysical research communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Patricia UychocoSan Francisco State University, Department of Chemistry and Biochemistry, San Francisco, CA, USA.
Karolina A MajorekUniversity of Virginia, Department of Molecular Physiology and Biological Physics, Charlottesville, VA, USA.
Ashley N IvesPacific Northwest National Laboratory, Environmental Molecular Sciences Laboratory, Richland, WA, USA.
Van Thi Bich LeSan Francisco State University, Department of Chemistry and Biochemistry, San Francisco, CA, USA.
Pamela L Caro De SilvaSan Francisco State University, Department of Chemistry and Biochemistry, San Francisco, CA, USA.
Vanessa L PaurusPacific Northwest National Laboratory, Environmental Molecular Sciences Laboratory, Richland, WA, USA.
Isaac Kwame AttahPacific Northwest National Laboratory, Environmental Molecular Sciences Laboratory, Richland, WA, USA.
Mary S LiptonPacific Northwest National Laboratory, Environmental Molecular Sciences Laboratory, Richland, WA, USA.
Wladek MinorUniversity of Virginia, Department of Molecular Physiology and Biological Physics, Charlottesville, VA, USA.
Misty L KuhnSan Francisco State University, Department of Chemistry and Biochemistry, San Francisco, CA, USA; Pacific Northwest National Laboratory, Earth and Biological Sciences Division, Richland, WA, USA. Electronic address: mkuhn@sfsu.edu.

Funding

User Training & OutreachP30GM138396 · NIGMS · UCHICAGO ARGONNE, LLC · PI ROBERT F. FISCHETTI, JANET L. SMITH · 2020 to 2026
$34.3M
Investigating the structure, function, and regulation of polyamine acetyltransferasesR35GM133506 · NIGMS · SAN FRANCISCO STATE UNIVERSITY · PI Misty Kuhn · 2019 to 2026
$2.9M
Reproducible, Unbiased Ligand Identification Assisted by Artificial Intelligence and Development of Ligand Reference LibrariesR01GM132595 · NIGMS · UNIVERSITY OF VIRGINIA · PI MINOR, WLADEK · 2019 to 2022
$2.3M
NIGMS NIH HHS P30 GM138396NIGMS NIH HHS R01 GM132595NIGMS NIH HHS R35 GM133506
6 · The paper itself

Abstract

Polyamines within the cell are tightly regulated by spermidine/spermine N-acetyltransferase (SSAT) enzymes. While several SSATs have been investigated in different bacterial species, there is still a significant gap in knowledge about which proteins are functional SSATs in many organisms. For example, while it is known that Pseudomonas aeruginosa synthesizes the polyamine spermidine, the SSAT that acetylates this molecule and its importance in regulating intracellular polyamines remains unknown. We previously identified a candidate Gcn5-related N-acetyltransferase (GNAT) protein from P. aeruginosa (PA2271) that could fulfill this role since it acetylates spermidine, but no further studies were conducted. Here, we explored the structure/function relationship of the PA2271 protein by determining its X-ray crystal structure and performing enzyme kinetics assays. We also identified active site residues that are essential for catalysis and substrate binding. As the study progressed, we encountered results that led us to explore the importance of four cysteine residues on enzyme activity and disulfide bond formation or modification of cysteine residues. We found these cysteine residues in PA2271 are important for protein solubility and activity, and there is an interrelationship between cysteine residues that contribute to these effects. Furthermore, we also found disulfide bonds could form between C

Indexed as

AcetyltransferasesBacterial ProteinsCysteineProtein Processing, Post-TranslationalPseudomonas aeruginosaAmino Acid SequenceCatalytic DomainCrystallography, X-RayKineticsModels, MolecularProtein ConformationAcetyltransferasesBacterial ProteinsCysteineCysteine Post-Translational ModificationsDisulfide BondsGcn5-related N-acetyltransferase (GNAT)Loss of enzyme activity with freeze/thaw cyclesPolyaminePseudomonas aeruginosaSpermidine

Identifiers

PMID39826527
PMCPMC11863989

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Registered trials

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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.