James N. Blaza

This paper reports a 13-subunit c-ring in the Chlamydomonas chloroplast ATP synthase, which lowers the H+/ATP cost of carbon fixation compared to the 14-subunit structure in spinach.

The paper identifies functional and structural differences among three GH172 arabinofuranosidases from Dysgonomonas gadei using synthetic substrates, covalent inhibitors, and structural analysis.

Fluorescent tagging of 160 proteins in the seaweed Ulva maps its carbon-concentrating pathway, and identifies SUPA1, a Rubisco linker that binds only four of eight sites.

This study identifies quinone-transporting filaments in Bacillus subtilis as an alternative to membrane invaginations for expanding respiratory capacity in Gram-positive bacteria.

This study determines the structure of TbAQP2 bound to drugs and glycerol, revealing how mutations in the channel lead to drug resistance in Trypanosoma brucei.

The paper measures bioenergetic processes during bacterial spore germination, finding early energisation of the electron transport chain and a role for Yth oxidase in rehydration.

This study uses remission spectroscopy to show bedaquiline inhibits ATP synthase in mycobacteria, redirecting electron flux through cytochrome bd oxidase and increasing O2 consumption, without uncoupling.

The paper identifies a conserved 10-transmembrane helical fold in diverse acyl transferases, defining the TmAT superfamily involved in transmembrane acyl-group transfer.

The paper uses cryogenic electron tomography to reveal a stargate mechanism for Microviridae genome delivery, showing it is universal across the family.

The paper identifies a conserved linker protein from Chlorella that can phase separate Rubisco in Chlamydomonas and some plants, enabling cross-species pyrenoid formation.

The paper identifies a protein interaction network in the diatom pyrenoid, revealing a structural shell critical for CO2 fixation and suggesting convergent evolution with prokaryotic carboxysomes.

The paper presents the cryo-EM structure of the CDK2-cyclin A-CDC25A complex, revealing key interactions and suggesting potential binding partners for CDC25A.

The paper identifies a new bacterial ribosome hibernation factor, Balon, and shows it is evolutionarily linked to eukaryotic translation factors, revealing a novel stress response mechanism.