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Cysteine Mutagenesis of a Group II Intron-Encoded Protein Supports Splicing, Mobility, and Site-Specific Labeling. 一类内含子编码蛋白的半胱氨酸突变支持剪接、迁移和位点特异性标记。
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-29 DOI: 10.1021/acs.biochem.5c00382
Jasmine A Harper, Sarah A Starcovic, Neil Billington, Aaron R Robart
{"title":"Cysteine Mutagenesis of a Group II Intron-Encoded Protein Supports Splicing, Mobility, and Site-Specific Labeling.","authors":"Jasmine A Harper, Sarah A Starcovic, Neil Billington, Aaron R Robart","doi":"10.1021/acs.biochem.5c00382","DOIUrl":"10.1021/acs.biochem.5c00382","url":null,"abstract":"<p><p>Group II introns are self-splicing ribozymes that excise themselves from precursor RNA and integrate into new DNA locations through retromobility. Splicing is facilitated by an intron-encoded protein (IEP), a multidomain reverse transcriptase that enhances ribozyme activity and promotes formation of lariat intron-IEP ribonucleoprotein (RNP) complexes. In this study, we examined the role of conserved cysteine residues in the IEP of the group IIC intron <i>Ta.it.</i>I1 from the thermophile <i>Thermoanaerobacter italicus</i> by generating cysteine-to-methionine mutants. All variants retained near wild-type splicing efficiency, indicating that cysteine substitution does not impair maturase function. A mutation in the thumb domain significantly enhanced reverse transcription (RT) activity, whereas substitutions flanking the YADD catalytic motif led to reduced activity. Despite these variable RT effects, all mutants retained the ability to complete both steps of forward intron self-splicing and subsequently perform reverse splicing into DNA targets. Complete removal of native cysteines enabled site-specific fluorescent labeling of the IEP using maleimide-thiol chemistry without disrupting splicing or retromobility. Labeled IEPs retained activity and were successfully used to monitor RNA binding and RNP assembly under native conditions. These findings highlight the structural flexibility of IEP-intron interactions and demonstrate that site-specific IEP labeling enables real-time visualization of RNP assembly and dynamics.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":" ","pages":""},"PeriodicalIF":3.0,"publicationDate":"2025-08-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144935621","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
SwsB Acts as a Muramic-δ-lactam Cyclase in Bacillus subtilis Spore Peptidoglycan Synthesis SwsB在枯草芽孢杆菌孢子肽聚糖合成中作为胞浆-δ-内酰胺环化酶。
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-28 DOI: 10.1021/acs.biochem.5c00449
Madison E. Hopkins, Zachary Yasinov, Mark J. Fakler, Grace E. Wilde, Katherine G. Wetmore and Michael A. Welsh*, 
{"title":"SwsB Acts as a Muramic-δ-lactam Cyclase in Bacillus subtilis Spore Peptidoglycan Synthesis","authors":"Madison E. Hopkins,&nbsp;Zachary Yasinov,&nbsp;Mark J. Fakler,&nbsp;Grace E. Wilde,&nbsp;Katherine G. Wetmore and Michael A. Welsh*,&nbsp;","doi":"10.1021/acs.biochem.5c00449","DOIUrl":"10.1021/acs.biochem.5c00449","url":null,"abstract":"<p >The cortex layer of the peptidoglycan cell wall surrounding bacterial spores contains a modified sugar, muramic-δ-lactam, that is essential for spore germination. Genetic evidence has linked the conserved enzyme SwsB to the muramic-δ-lactam biosynthetic pathway. SwsB belongs to a large family of metal-dependent deacetylases, but its function is unclear because a putative catalytic residue is mutated. We have used native cortex peptidoglycan substrates to show that SwsB acts not as a deacetylase but as a monofunctional muramic-δ-lactam cyclase, the first enzyme reported with this activity. SwsB is remarkable in that it catalyzes lactam synthesis by direct intramolecular condensation of a carboxylate and primary amine with no apparent requirement for chemical energy input. SwsB will accept a minimal peptidoglycan substrate and, surprisingly, does not require a transition metal ion cofactor for cyclase activity. Our results suggest an <i>in vivo</i> role for SwsB and lay the foundation for mechanistic and structural studies of an unusual enzyme.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":"64 18","pages":"3814–3818"},"PeriodicalIF":3.0,"publicationDate":"2025-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12444981/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144935583","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Rieske Oxygenases: Powerful Models for Understanding Nature’s Orchestration of Electron Transfer and Oxidative Chemistry Rieske加氧酶:理解电子转移和氧化化学的自然协调的强大模型。
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-28 DOI: 10.1021/acs.biochem.5c00369
Hui Miao,  and , Sandy Schmidt*, 
{"title":"Rieske Oxygenases: Powerful Models for Understanding Nature’s Orchestration of Electron Transfer and Oxidative Chemistry","authors":"Hui Miao,&nbsp; and ,&nbsp;Sandy Schmidt*,&nbsp;","doi":"10.1021/acs.biochem.5c00369","DOIUrl":"10.1021/acs.biochem.5c00369","url":null,"abstract":"<p >Rieske oxygenases (ROs) are a diverse family of nonheme iron enzymes that catalyze a wide array of oxidative transformations in both catabolic and biosynthetic pathways. Their catalytic repertoire spans dioxygenation, monooxygenation, oxidative <i>N</i>- and <i>O</i>-dealkylation, desaturation, sulfoxidation, C–C bond formation, <i>N</i>-oxygenation, and C–N bond cleavage─reactions that are often challenging to achieve selectively through synthetic methods. These diverse functions highlight the increasing importance of ROs in natural product biosynthesis and establish them as promising candidates for biocatalytic applications. Despite extensive study, our understanding of how ROs orchestrate these diverse reactions at the molecular level remains incomplete. In particular, the transient, dynamic nature of electron transfer events and the limited structural characterization of oxygen-bound intermediates hinder our understanding of how structural features govern electron transfer efficiency, O<sub>2</sub> activation, and the origins of their catalytic diversity. Recent findings challenge traditional views of the RO catalytic cycle and underscore the importance of integrating static structural data with dynamic studies of redox interactions. In this Perspective, we explore emerging insights into the structural and mechanistic basis of RO function. We focus on how the architecture of the oxygenase component shapes reactivity, electron transfer, and redox partner interactions. Finally, we discuss current limitations and future opportunities in harnessing ROs for biocatalysis, emphasizing the potential of engineering approaches─particularly the optimization of redox partner compatibility─to expand their functional utility.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":"64 18","pages":"3801–3813"},"PeriodicalIF":3.0,"publicationDate":"2025-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12445004/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144935649","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
A Structurally Divergent Class Ia Ribonucleotide Reductase from a Tick-Borne Pathogen 一种结构不同的蜱传病原体的Ia类核糖核苷酸还原酶。
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-28 DOI: 10.1021/acs.biochem.5c00316
Olivia M. Peduzzi, Gavin M. Palowitch, John P. Gajewski, Kai Hu, Alyssa Wheeler, Tatiana N. Laremore, Steve Silletti, Elizabeth A. Komives, Benjamin D. Allen, Alexey Silakov, Carsten Krebs, J. Martin Bollinger Jr.*, Chi-Yun Lin* and Amie K. Boal*, 
{"title":"A Structurally Divergent Class Ia Ribonucleotide Reductase from a Tick-Borne Pathogen","authors":"Olivia M. Peduzzi,&nbsp;Gavin M. Palowitch,&nbsp;John P. Gajewski,&nbsp;Kai Hu,&nbsp;Alyssa Wheeler,&nbsp;Tatiana N. Laremore,&nbsp;Steve Silletti,&nbsp;Elizabeth A. Komives,&nbsp;Benjamin D. Allen,&nbsp;Alexey Silakov,&nbsp;Carsten Krebs,&nbsp;J. Martin Bollinger Jr.*,&nbsp;Chi-Yun Lin* and Amie K. Boal*,&nbsp;","doi":"10.1021/acs.biochem.5c00316","DOIUrl":"10.1021/acs.biochem.5c00316","url":null,"abstract":"<p >Ribonucleotide reductases (RNRs) generate 2′-deoxynucleotides for DNA biosynthesis, a reaction essential to all life. Class I RNRs have two subunits, α and β. α binds and reduces the substrate, whereas β oxidizes one of the cysteines in α to a C3′–H-bond-cleaving thiyl radical to begin the reaction. The α-Cys oxidant in β is variously a tyrosyl radical (Y<sup>•</sup>) generated by a diiron or dimanganese cluster, a high-valent dimetal cluster [Mn(IV)/Fe(III) or Mn<sub>2</sub>(IV/III)], or a dihydroxylphenylalanine (DOPA) radical that operates without need of a transition metal. The metal (in)dependence of the Cys oxidant in β correlates loosely with sequence-similarity groupings. We show here that <i>Francisella hispaniensis</i> (<i>Fh</i>) β, which lies within an uncharacterized sequence cluster that contains orthologs from multiple human pathogens, harbors a Fe<sub>2</sub>(III/III)/Y<sup>•</sup> cofactor, as in class Ia RNRs from eukaryotes and <i>Escherichia coli</i>. <i>Fh</i> β has several unusual structural features that may reflect adaptation to the bacterium’s environment(s). In its apo form, an unwound helix everts a metal ligand toward solvent, and the radical-harboring Y points away from the diiron cluster. An additional aromatic residue (W194), conserved within the sequence cluster, is found close to the universally conserved W37, which is thought to mediate α-Cys oxidation in all class I enzymes. The Y<sup>•</sup> in resting β is remarkably resistant to reduction by hydroxyurea but becomes 8000 times more sensitive when β is engaged in turnover with α. These structural and functional distinctions could be counter measures against host redox defenses that would target the pathogen’s RNR and its cofactor.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":"64 18","pages":"3935–3955"},"PeriodicalIF":3.0,"publicationDate":"2025-08-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144935937","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
BPTF Target Engagement by Acetylated H2A.Z Photoaffinity Probes 乙酰化H2A击中BPTF目标。Z光亲和探针。
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-27 DOI: 10.1021/acs.biochem.5c00378
Kerstin E. Peterson, Noelle M. Olson, Dani J. Dahlseid, Jacklyn M. Artymiuk, Luke Erber, Francisca N. L. Vitorino, Renee Dean, Joseph W. Landry, Natalia Y. Tretyakova, Benjamin A. Garcia and William C. K. Pomerantz*, 
{"title":"BPTF Target Engagement by Acetylated H2A.Z Photoaffinity Probes","authors":"Kerstin E. Peterson,&nbsp;Noelle M. Olson,&nbsp;Dani J. Dahlseid,&nbsp;Jacklyn M. Artymiuk,&nbsp;Luke Erber,&nbsp;Francisca N. L. Vitorino,&nbsp;Renee Dean,&nbsp;Joseph W. Landry,&nbsp;Natalia Y. Tretyakova,&nbsp;Benjamin A. Garcia and William C. K. Pomerantz*,&nbsp;","doi":"10.1021/acs.biochem.5c00378","DOIUrl":"10.1021/acs.biochem.5c00378","url":null,"abstract":"<p >Histone variant H2A.Z has been increasingly associated with cancer progression, including cancers characterized by the dysregulated function of the epigenetic reader protein BPTF (bromodomain and PHD finger containing transcription factor). Despite this association, a direct interaction between acetylated H2A.Z and BPTF has not been validated in a physiological context, given the weak bromodomain-histone tail affinity. Here, we developed photoaffinity acetylated histone probes based on differentially acetylated H2A.Z isoforms I and II with an N-terminal diazirine and a C-terminal biotin tag for covalently capturing and enriching BPTF and new interactors. Photo-crosslinking experiments followed by SDS-PAGE revealed that recombinant BPTF bromodomain (BPTF BD) directly interacts with both isoforms of H2A.Z in an affinity-dependent and acetyl-lysine binding pocket-specific manner. In nuclear lysates prepared from A549 non-small cell lung cancer cells, acetylated H2A.Z isoform probes enriched endogenous BPTF as a photo-crosslinking target, but to a lesser extent than the canonical partner, H4K16ac. Finally, to determine the natural acetylation patterns of H2A.Z in a human cancer cell line, we used bottom-up proteomics to quantify the levels and patterns of acetylation on H2A.Z from A549 cells. Mono- and diacetylation were the predominant acetylation patterns identified, with patterns containing acetylation sites K4ac, K7ac, K11ac, and K15ac. These results indicate that our photoaffinity probes can capture transient epigenetic protein–protein interactions, while optimization of conditions for interactome analysis of these transient interactions will be necessary for identifying additional epigenetic regulators of H2A.Z.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":"64 18","pages":"3872–3885"},"PeriodicalIF":3.0,"publicationDate":"2025-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144935946","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Stuffed Epimerase Domains of Pyochelin Biosynthesis are Defunct Methyltransferases Pyochelin生物合成填充的epimase结构域是失效的甲基转移酶。
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-26 DOI: 10.1021/acs.biochem.5c00172
Trey A. Ronnebaum, Kathleen M. Meneely, Geoff P. Horsman, Thomas E. Prisinzano and Audrey L. Lamb*, 
{"title":"Stuffed Epimerase Domains of Pyochelin Biosynthesis are Defunct Methyltransferases","authors":"Trey A. Ronnebaum,&nbsp;Kathleen M. Meneely,&nbsp;Geoff P. Horsman,&nbsp;Thomas E. Prisinzano and Audrey L. Lamb*,&nbsp;","doi":"10.1021/acs.biochem.5c00172","DOIUrl":"10.1021/acs.biochem.5c00172","url":null,"abstract":"<p >Bacteria and fungi use nonribosomal peptide synthetases (NRPSs) to generate secondary metabolites called nonribosomal peptides (NRPs). A common feature of NRPs is the incorporation of <span>D</span>-stereocenter amino acids, which enhance chemical functionality and confer resistance to proteolytic degradation. Typically, these stereochemical inversions arise from dedicated epimerase domains, which are well-characterized. However, 2-hydroxyphenylthiazoline-containing natural products lack these conventional tailoring domains and are instead proposed to utilize noncanonical epimerase domains embedded, or “stuffed”, within the mobile loop of NRPS adenylation domains. The stereochemistry of the final natural product does not align with the absence or presence of the stuffed epimerase domain, so we examined the adenylation-epimerase didomains of 2-hydroxyphenylthiazoline siderophores from <i>Pseudomonas aeruginosa</i> (pyochelin, <i>R</i> stereochemistry at 4’) and <i>Streptomyces venezuelae</i> (watasemycin, <i>S</i> at 4’). For comparison, we also examined the biosynthesis of enantiopyochelin (<i>S</i> at 4’) by the homologous enzyme from <i>Pseudomonas protegens</i>, which lacks the stuffed epimerase domain. Substrate and product analogs were synthesized to probe the epimerase chemistry. While the variants performed adenylation chemistry, epimerase activity was not enzymatically catalyzed. Indeed, racemization was spontaneous for the 2-hydroxyphenylthiazoline ethyl ester analogues and for intermediates isolated from the enzymes. These data suggest that noncanonical stuffed epimerase domains of 2-hydroxyphenylthiazoline natural products are catalytically defunct methyltransferases and possibly an evolutionary remnant.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":"64 18","pages":"3919–3934"},"PeriodicalIF":3.0,"publicationDate":"2025-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144935647","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Time-Resolved Infrared Evidence for Protein Conformational Changes During the Dark-Rearrangement Process of Photosystem II Photoactivation: A Comparative Study of Solution and Crystal Samples 光系统II光激活暗重排过程中蛋白质构象变化的时间分辨红外证据:溶液和晶体样品的比较研究
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-21 DOI: 10.1021/acs.biochem.5c00426
Yuki Kato*, Kazuki Ogura, Yoshiki Nakajima, Jian-Ren Shen and Takumi Noguchi*, 
{"title":"Time-Resolved Infrared Evidence for Protein Conformational Changes During the Dark-Rearrangement Process of Photosystem II Photoactivation: A Comparative Study of Solution and Crystal Samples","authors":"Yuki Kato*,&nbsp;Kazuki Ogura,&nbsp;Yoshiki Nakajima,&nbsp;Jian-Ren Shen and Takumi Noguchi*,&nbsp;","doi":"10.1021/acs.biochem.5c00426","DOIUrl":"https://doi.org/10.1021/acs.biochem.5c00426","url":null,"abstract":"<p >The catalytic site of photosynthetic water oxidation, the water-oxidizing complex (WOC), which contains the Mn<sub>4</sub>CaO<sub>5</sub> cluster as its inorganic core, is assembled in photosystem II (PSII) through a light-driven process known as photoactivation. Despite extensive study, the detailed molecular mechanism underlying photoactivation remains elusive. Here, we investigated the mechanism of photoactivation by focusing on the “dark rearrangement process” that occurs following the first flash illumination, using time-resolved Fourier transform infrared (FTIR) measurements of apo-WOC PSII both in crystals, where the protein conformation remains nearly unchanged upon Mn depletion, and in solution, where Mn removal induces substantial conformational changes. Time-resolved FTIR spectra of apo-WOC PSII in solution, following single-flash illumination in the presence of Mn<sup>2+</sup>, revealed two distinct decay phases. The fast phase was characterized by increased relative intensities of amide I bands accompanied by shifts in carboxylate stretching bands, while the slow phase exhibited minimal spectral changes. In contrast, FTIR spectra of apo-WOC PSII in crystals showed only a single slow decay phase, with a time constant comparable to that of the slow component in solution, and with negligible change in spectral shape. This striking contrast between PSII in solution and in crystals provides definitive evidence that significant protein conformational changes, accompanied by Mn<sup>3+</sup> relocation via carboxylate groups, occur during the dark rearrangement process following the initial photooxidation of Mn<sup>2+</sup> under physiological conditions.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":"64 17","pages":"3781–3789"},"PeriodicalIF":3.0,"publicationDate":"2025-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144924790","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Fluorescence Light-Up of G4 DNA Structures Using Azlactone-Based Probes 基于阿兹内酯探针的G4 DNA结构荧光发光研究
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-20 DOI: 10.1021/acs.biochem.5c00280
Annyesha Biswas, Nitesh Ayare, Y. Dilnawaj, Vipin Kumar Mishra and P. I. Pradeepkumar*, 
{"title":"Fluorescence Light-Up of G4 DNA Structures Using Azlactone-Based Probes","authors":"Annyesha Biswas,&nbsp;Nitesh Ayare,&nbsp;Y. Dilnawaj,&nbsp;Vipin Kumar Mishra and P. I. Pradeepkumar*,&nbsp;","doi":"10.1021/acs.biochem.5c00280","DOIUrl":"https://doi.org/10.1021/acs.biochem.5c00280","url":null,"abstract":"<p >G-rich sequences of DNA and RNA can form G-quadruplex (G4) structures, modulating a myriad of biological processes. Thus, it is imperative to understand the structural topologies, location, and function of G4s under cell-free conditions and in the cellular milieu. In the present study, we report three small-molecule fluorescent probes based on azlactones (<b>AZL1</b>-<b>3</b>) that significantly light up (∼65–135-fold) the parallel topology of the <i>c-MYC</i>, <i>c-KIT1</i>, and mitochondrial HRCC G4 DNAs. The lead probe AZL1 exhibits a 2:1 binding stoichiometry with <i>c-KIT1</i> G4 DNA by accessing the 5′ and 3′-G-quartets. It shows limited cytotoxicity and exhibits fluorescence light-up in the cytoplasm of the HeLa cells due to weak colocalization with the mitochondrial G4 DNAs along with strong colocalization with lipid droplets. These results demonstrate that azlactone-based probes are useful tools to sense G4 structures in a cell-free environment and could be further engineered for potential bioimaging and diagnostic applications.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":"64 17","pages":"3706–3717"},"PeriodicalIF":3.0,"publicationDate":"2025-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144924778","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Raman Spectroscopy and Imaging Reveal the Effect of β-Carotene Supplementation on Brain Cancer Cells 拉曼光谱和成像揭示了补充β-胡萝卜素对脑癌细胞的影响
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-20 DOI: 10.1021/acs.biochem.5c00231
Karolina Jarczewska, Monika Kopeć, Halina Abramczyk and Jakub Maciej Surmacki*, 
{"title":"Raman Spectroscopy and Imaging Reveal the Effect of β-Carotene Supplementation on Brain Cancer Cells","authors":"Karolina Jarczewska,&nbsp;Monika Kopeć,&nbsp;Halina Abramczyk and Jakub Maciej Surmacki*,&nbsp;","doi":"10.1021/acs.biochem.5c00231","DOIUrl":"https://doi.org/10.1021/acs.biochem.5c00231","url":null,"abstract":"<p >Dietary β-carotene is the most common carotenoid in the world. Naturally occurs in vegetables and fruits (e.g., carrots, tomatoes). Recently, β-carotene has been studied for its effects on the human body; however, the effect of this carotenoid on brain tumor metabolism at the cellular level is still unknown. Here, we consider whether β-carotene influences brain tumor cell metabolism and, if so, whether this effect stimulates or inhibits tumor growth. To find out the effect of β-carotene on brain cells (normal human astrocytes, astrocytoma, and glioblastoma), we applied Raman spectroscopy and imaging. We focused our analysis on biological changes in particular cell organelles such as the nucleus, mitochondria, lipid droplets/endoplasmic reticulum, and cytoplasm. Our Raman results demonstrated that cancer cell metabolism is altered following β-carotene supplementation, as reflected in changes to Raman bands associated with cytochrome <i>c</i> (1310 and 1583 cm<sup>–</sup><sup>1</sup>), lipids (1337 and 1444 cm<sup>–</sup><sup>1</sup>), and proteins (1337 and 1654 cm<sup>–</sup><sup>1</sup>). The response to supplementation is different not only for normal cells compared to cancer cells (the effects vary depending on the cell type) but also for supplementation timing and doses.</p>","PeriodicalId":28,"journal":{"name":"Biochemistry Biochemistry","volume":"64 17","pages":"3745–3759"},"PeriodicalIF":3.0,"publicationDate":"2025-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5c00231","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144924733","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Biochemical Applications of Microbial Rare Glycan Biosynthesis, Recognition, and Sequencing 微生物稀有聚糖生物合成、识别和测序的生化应用
IF 3 3区 生物学
Biochemistry Biochemistry Pub Date : 2025-08-20 DOI: 10.1021/acs.biochem.5c00338
Joanna Joo, Andrea Koid, Hanee Kim, Antara Ghosh, Seayoung Lee, Mia Sheshova and Tania J. Lupoli*, 
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