ArticleThe Biochemical journal2025
The ClpA chaperone and the two adaptor proteins modulate the fate of the model substrate tagged with a SsrA-degron of Leptospira.
Article in The Biochemical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial caseinolytic protease (Clp) chaperone-protease complexes are essential for the degradation of misfolded and aggregated protein substrates. The spirochaete Leptospira interrogans possesses a set of Clp adaptor proteins (ClpS1 and ClpS2) and chaperones (ClpX, ClpA and ClpC), which are believed to associate with two distinct isoforms of ClpP (ClpP1 and ClpP2). This study explores the structural and functional properties of LinClpA, LinClpS1 and LinClpS2 derived from L. interrogans. LinClpA, a 740-amino acid protein, features an N-terminal domain and two AAA+ ATPase domains (D-I and D-II), containing conserved motifs critical for ATP binding and hydrolysis. LinClpS1 and LinClpS2 exhibit similar structures, yet they possess distinct binding pockets for N-degron substrates. Biochemical assays indicate that the N-domain-deleted variant of LinClpA (LinClpAΔN) exhibits a nucleotide-induced oligomerization tendency similar to LinClpA's but demonstrates higher ATPase activity. Interaction studies have shown that LinClpA's ATPase activity is enhanced in the presence of LinClpP isoforms and inhibited by LinClpS isoforms. In contrast, the activity of LinClpAΔN remained unaffected by LinClpS1 and LinClpS2, highlighting the significance of the N-domain of LinClpA in adaptor protein interactions. Furthermore, the study predicted and evaluated the role of the C-degron tag called small stable RNA A in facilitating protein degradation by the L. interrogans ClpAP1P2 machinery.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.