DLST

Last update 08 May 2025

Basic Info

Synonyms

2-oxoglutarate dehydrogenase complex component E2, dihydrolipoamide S-succinyltransferase, Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex

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Introduction

Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex. The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711, PubMed:30929736). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711).

100 Clinical Results associated with DLST

100 Translational Medicine associated with DLST

0 Patents (Medical) associated with DLST

261

Literatures (Medical) associated with DLST

01 Jun 2025·Journal of Structural Biology: X

Protein identification using Cryo-EM and artificial intelligence guides improved sample purification

Article

Author: Borst, Andrew J ; Weidle, Connor ; Pyles, Harley ; Carr, Kenneth D ; Goodson, Alex ; Courbet, Alexis ; Zambrano, Dane Evan D ; King, Neil P ; Eisenach, Helen E

Protein purification is essential in protein biochemistry, structural biology, and protein design, enabling the determination of protein structures, the study of biological mechanisms, and the characterization of both natural and de novo designed proteins. However, standard purification strategies often encounter challenges, such as unintended co-purification of contaminants alongside the target protein. This issue is particularly problematic for self-assembling protein nanomaterials, where unexpected geometries may reflect novel assembly states, cross-contamination, or native proteins originating from the expression host. Here, we used an automated structure-to-sequence pipeline to first identify an unknown co-purifying protein found in several purified designed protein samples. By integrating cryo-electron microscopy (Cryo-EM), ModelAngelo's sequence-agnostic model-building, and Protein BLAST, we identified the contaminant as dihydrolipoamide succinyltransferase (DLST). This identification was validated through comparisons with DLST structures in the Protein Data Bank, AlphaFold 3 predictions based on the DLST sequence from our E. coli expression vector, and traditional biochemical methods. The identification informed subsequent modifications to our purification protocol, which successfully excluded DLST from future preparations. To explore the potential broader utility of this approach, we benchmarked four computational methods for DLST identification across varying resolution ranges. This study demonstrates the successful application of a structure-to-sequence protein identification workflow, integrating Cryo-EM, ModelAngelo, Protein BLAST, and AlphaFold 3 predictions, to identify and ultimately help guide the removal of DLST from sample purification efforts. It highlights the potential of combining Cryo-EM with AI-driven tools for accurate protein identification and addressing purification challenges across diverse contexts in protein science.

01 Apr 2025·International Dental Journal

GLS as a Key Cuproptosis-Related Gene in Periodontitis: Insights from Single-Cell RNA Sequencing

Article

Author: Xiuan, Zhu ; Donglin, Zhang ; Wenjie, Wen

OBJECTIVEThe objective of this study is to investigate the role of cuproptosis-related genes (CRGs) in periodontitis using an integrative approach that combines single-cell RNA sequencing (scRNA-seq) and bioinformatic analyses. The study aims to elucidate the connection between copper-induced cell death (cuproptosis) and periodontitis, a prevalent chronic inflammatory oral disease that leads to tooth-supporting tissue damage and eventual tooth loss.METHODSDifferentially expressed genes (DEGs) were identified from the GSE10334 dataset, leading to the discovery of 14 differentially expressed CRGs associated with periodontitis. Subsequent application of least absolute shrinkage and selection operator (LASSO) regression and logistic regression analysis pinpointed three key CRGs: MTF1, GLS, and DLST. Single-cell sequencing data analysis was further conducted to explore the expression patterns of these genes, particularly GLS, within immune cells and their association with the immune cell network in periodontal tissues.RESULTSThe study revealed that GLS is widely expressed in immune cells and is closely linked to the complex immune cell interactions within periodontal tissues. This finding underscores GLS as a potential therapeutic target in the context of periodontitis, associated with cuproptosis. The integration of single-cell sequencing data highlighted the significant role of cuproptosis in the diversity and complexity of periodontitis pathogenesis.CONCLUSIONThis research advances the understanding of the crosstalk between periodontitis and cuproptosis, emphasising the role of CRGs, especially GLS, in periodontitis. Furthermore, this study on cuproptosis may contribute to future diagnostic and therapeutic strategies for periodontitis.

01 Mar 2025·Veterinary Medicine and Science

Capsular Typing and Molecular Characterization of Streptococcus agalactiae Strains Isolated From Bovine Mastitis in Iran

Article

Author: Tajbakhsh, Elahe ; HajiAhmadi, Pegah ; Momtaz, Hassan

ABSTRACTStreptococcus agalactiae infections may cause clinical or subclinical mastitis in dairy cows by invading the mammary gland. This research included the isolation of 29 strains of S. agalactiae from 425 milk samples obtained from cows affected by clinical mastitis in Chaharmahal and Bakhtiari province, Iran. The antimicrobial sensitivity of S. agalactiae strains was determined using 16 antibiotics from seven different classes. The epidemiological spread of S. agalactiae was determined by identifying the serotypes of isolates using multiplex PCR. In addition, the presence of antibiotic‐resistance genes and virulence genes were investigated to infer the pathogenicity and antibiotic resistance of S. agalactiae using the multiplex PCR method. A total of 29 strains of S. agalactiae, which constitute 6.82% of the samples, were identified based on phenotypic traits, biochemical properties and dltR gene amplification. Multiplex serotype polymerase chain reaction study showed that most of the isolates belonged to Type III serotype. Phenotypically, 100% of the isolated strains were resistant to tetracycline and penicillin. The frequency of resistance to beta‐lactams (penicillin and amoxicillin) was 100% and 82.75%. tetM, tetO and tetT genes, responsible for resistance to tetracyclines, were found in all samples, corresponding to the drug‐resistant phenotype. Among the genes related to the virulence factor, 100% of the isolates had the dlts gene. The examination of virulence genes revealed that the majority of isolates included the cfb, pavA and scPb genes. This data has the potential to assist in the prevention and management of mastitis and enhance our comprehension of epidemiological patterns in dairy cows affected by S. agalactiae in Chaharmahal and Bakhtiari province.

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