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Molecular recognition of the promoter DNA signature sequence by Hms1p.
Int J Biol Macromol
January 2025
MOE Key Laboratory for Membraneless Organelles and Cellular Dynamics, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, China. Electronic address:
Transcriptional regulation of sterol biosynthetic genes is mediated by conserved sterol-regulatory element binding proteins (SREBPs) in human pathogenic fungi, however, its homolog in S. cerevisiae regulate filamentous growth during stress conditions. These pseudohyphal growths might be associated with the expression of MEP2 gene in response to ammonium limitation.
View Article and Find Full Text PDFMolecular insights into a distinct class of terpenoid cyclases.
Nat Commun
January 2025
State Key Laboratory of Biocatalysis and Enzyme Engineering, Hubei Hongshan Laboratory, School of Life Sciences, Hubei University, Wuhan, China.
Article Synopsis
- Terpenoid cyclases (TCs) are crucial for producing diverse natural compounds, with the BcABA3 enzyme from the fungus Botrytis cinerea representing a unique type that deviates from typical TCs.
- Crystal structures of BcABA3 and related enzymes show they have an all-α-helix fold and interact with specific substrates through a unique binding mechanism.
- Findings suggest significant potential for exploring more uncharacterized terpenoids synthesized by these enzymes, highlighting the need for further research in this area.
Introducing glutamic acid residues to acyl-ACP reductase to enhance alka(e)ne production in Escherichia coli: Computer-aided design and subsequent experimental validation.
Biochem Biophys Res Commun
January 2025
Department of Chemical Engineering, Osaka Metropolitan University, 1-1 Gakuen-cho, Naka-ku, Sakai, Osaka, 599-8531, Japan. Electronic address:
Acyl-acyl carrier protein (acyl-ACP) reductase (AAR) is a crucial enzyme in alka(e)ne production by recombinant Escherichia coli (E. coli). Engineered AAR expressed in E.
View Article and Find Full Text PDFPolar Networks Mediate Ion Conduction of the SARS-CoV-2 Envelope Protein.
J Am Chem Soc
December 2024
Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, Massachusetts 02139, United States.
The SARS-CoV-2 E protein conducts cations across the cell membrane to cause pathogenicity to infected cells. The high-resolution structures of the E transmembrane domain (ETM) in the closed state at neutral pH and in the open state at acidic pH have been determined. However, the ion conduction mechanism remains elusive.
View Article and Find Full Text PDFCryo-EM Detection of AMPylated Histidine Implies Covalent Catalysis in AMPylation Mediated by a Bacterial Effector.
J Mol Biol
December 2024
Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA. Electronic address:
AMPylation is a post-translational modification (PTM) whereby adenosine monophosphate (AMP) from adenosine triphosphate (ATP) is transferred onto protein hydroxyl groups of serine, threonine, or tyrosine. Recently, an actin-dependent AMPylase namely LnaB from the bacterial pathogen Legionella pneumophila was found to AMPylate phosphate groups of phosphoribosylated ubiquitin and Src family kinases. LnaB represents an evolutionarily distinct family of AMPylases with conserved active site Ser-His-Glu residues.
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