Melisa Lázaro

ORCID: 0000-0002-9603-9115
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About
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Research Areas
  • Enzyme Structure and Function
  • Amino Acid Enzymes and Metabolism
  • RNA and protein synthesis mechanisms
  • RNA modifications and cancer
  • Autophagy in Disease and Therapy
  • Mitochondrial Function and Pathology
  • Biotin and Related Studies
  • Photosynthetic Processes and Mechanisms
  • Bacterial Genetics and Biotechnology
  • Cellular transport and secretion
  • DNA Repair Mechanisms
  • Calcium signaling and nucleotide metabolism
  • RNA Research and Splicing
  • Advanced Electron Microscopy Techniques and Applications
  • Endoplasmic Reticulum Stress and Disease
  • Cancer-related Molecular Pathways
  • Alcoholism and Thiamine Deficiency
  • Prion Diseases and Protein Misfolding
  • GABA and Rice Research
  • Protein Structure and Dynamics
  • Force Microscopy Techniques and Applications
  • Metalloenzymes and iron-sulfur proteins
  • Lysosomal Storage Disorders Research

CIC bioGUNE
2010-2024

University of Vienna
2022

Universidad de Zaragoza
1991

During protein synthesis, tRNAs and mRNA move through the ribosome between aminoacyl (A), peptidyl (P), exit (E) sites of in a process called translocation. Translocation is accompanied by displacement on large ribosomal subunit toward hybrid A/P P/E states rotational movement (ratchet) subunits relative to one another. So far, structure ratcheted state has been observed only when translation factors were bound ribosome. Using cryo-electron microscopy classification, we show here that...

10.1073/pnas.0809587105 article EN Proceedings of the National Academy of Sciences 2008-10-30

Abstract In macroautophagy, the autophagosome (AP) engulfs portions of cytoplasm to allow their lysosomal degradation. AP formation in humans requires concerted action ATG12 and LC3/GABARAP conjugation systems. The ATG12–ATG5-ATG16L1 or E3-like complex (E3 for short) acts as a ubiquitin-like E3 enzyme, promoting proteins anchoring membrane. Their role expansion process is still unclear, part because there are no studies comparing six family member roles under same conditions, also full human...

10.1007/s00018-023-04704-z article EN cc-by Cellular and Molecular Life Sciences 2023-02-01

The multidomain homotetrameric tumor suppressor p53 has two modes of binding dsDNA that are thought to be responsible for scanning and recognizing specific response elements (REs). C termini bind nonspecifically dsDNA. four DNA-binding domains (DBDs) REs have symmetric 10 base-pair sequences. bound a 20-bp RE the DBDs enveloping DNA, which is in center molecule surrounded by linker sequences tetramerization domain (Tet). We investigated electron microscopy structures DNA consisting with...

10.1073/pnas.1015520107 article EN Proceedings of the National Academy of Sciences 2010-12-22

The mitochondrial replicative helicase Twinkle is involved in strand separation at the replication fork of DNA (mtDNA). malfunction associated with rare diseases that include late onset myopathies, neuromuscular disorders and fatal infantile mtDNA depletion syndrome. We examined its 3D structure by electron microscopy (EM) small angle X-ray scattering (SAXS) built corresponding atomic models, which gave insight into first molecular architecture a full-length SF4 includes an N-terminal...

10.1093/nar/gkv189 article EN cc-by-nc Nucleic Acids Research 2015-03-30

Among transmissible spongiform encephalopathies or prion diseases affecting humans, sporadic forms such as Creutzfeldt-Jakob disease are the vast majority. Unlike genetic acquired of disease, these idiopathic occur seemingly due to a random event spontaneous misfolding cellular PrP (PrPC) into pathogenic isoform (PrPSc). Currently, molecular mechanisms that trigger and drive this event, which occurs in approximately one individual per million each year, remain completely unknown. Modelling...

10.1186/s40478-023-01640-8 article EN cc-by Acta Neuropathologica Communications 2023-09-07

Abstract Pyruvate carboxylase (PC) is a tetrameric enzyme that contains two active sites per subunit catalyze consecutive reactions. A mobile domain with an attached prosthetic biotin links both reactions, initial carboxylation and the subsequent carboxyl transfer to pyruvate substrate produce oxaloacetate. Reaction are at long distance, there several co-factors play as allosteric regulators. Here, using cryoEM we explore structure of PC tetramers focusing on conformational space oligomers....

10.1038/s41467-022-33987-2 article EN cc-by Nature Communications 2022-10-19

Abstract Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate composed of 180 kDa subunits (L-GDHs ) contain long N- and C-terminal segments flanking the catalytic core. Despite relevance L-GDHs bacterial physiology, lack structural data for these has limited progress functional studies. Here we show mycobacterial L-GDH (mL-GDH adopts a quaternary structure is radically different from related low molecular weight...

10.1038/s42003-021-02222-x article EN cc-by Communications Biology 2021-06-03

ABSTRACT Glutamate dehydrogenases (GDHs) catalyze the oxidative deamination of L-glutamate to 2-oxoglutarate using NAD(P) + as a cofactor. The large type GDHs (L-GDHs) displays dynamic homotetrameric architecture that alternates between open and closed states. catalytic mechanism role conformational changes L-GDHs in enzymatic function are unknown. Here, we explore by cryoEM structure space mycobacterial L-GDH composed 180 kDa subunits (mL-GDH ) when incubated with NAD . Classification...

10.1101/2024.12.26.630402 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-12-26

Summary Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate composed of 180 kDa subunits (L-GDHs ) contain long N- and C-terminal segments flanking the catalytic core. Despite relevance L-GDHs bacterial physiology, lack structural data for these has limited progress functional studies. Here we show mycobacterial L-GDH (mL-GDH adopts a quaternary structure is radically different from related low molecular weight...

10.1101/2020.11.14.381715 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2020-11-15

Abstract In macroautophagy, the autophagosome (AP) engulfs portions of cytoplasm to allow their lysosomal degradation. AP formation in humans requires concerted action ATG12 and LC3/GABARAP conjugation systems. The ATG12–ATG5-ATG16L1 (E3) complex acts as a ubiquitin-like E3 ligase enzyme, promoting protein anchoring membrane. role various proteins expansion process is still unclear, part because there are no studies comparing LC3/GABARAP-family member roles under same conditions, also full...

10.21203/rs.3.rs-1925210/v1 preprint EN cc-by Research Square (Research Square) 2022-08-24
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