A new type of phasin characterized by the presence of a helix-hairpin-helix domain is required for normal polyhydroxybutyrate accumulation and granule organization in Caulobacter crescentus
Por:
Salinas A.L., Osorio A., Legorreta-Hissner T., Lara-Martinez R., Jimenez-Garcia L.F., Camarena L., Poggio S.
Publicada:
1 ene 2023
Ahead of Print:
1 jul 2023
Resumen:
Bacteria frequently store excess carbon in hydrophobic granules of polyhydroxybutyrate (PHB) that in some growth conditions can occupy most of the cytoplasmic space. Different types of proteins associate to the surface of the granules, mainly enzymes involved in the synthesis and utilization of the reserve polymer and a diverse group of proteins known as phasins. Phasins have different functions, among which are regulating the size and number of the granules, modulating the activity of the granule-associated enzymes and helping in the distribution of the granules inside the cell. Caulobacter crescentus is an oligotrophic bacterium that shows several morphological and regulatory traits that allow it to grow in very nutrient-diluted environments. Under these conditions, storage compounds should be particularly relevant for survival. In this work, we show an initial proteomic characterization of the PHB granules and describe a new type of phasin (PhaH) characterized by the presence of an N-terminal hydrophobic helix followed by a helix-hairpin-helix (HhH) domain. The hydrophobic helix is required for maximal PHB accumulation and maintenance during the stationary phase while the HhH domain is involved in determining the size of the PHB granules and their distribution in the cell. © 2023 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.
Filiaciones:
Salinas A.L.:
Departamento de Biología Molecular y Biotecnología, Instituto de Ivestigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico
Osorio A.:
Departamento de Biología Molecular y Biotecnología, Instituto de Ivestigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico
Legorreta-Hissner T.:
Departamento de Biología Molecular y Biotecnología, Instituto de Ivestigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico
Lara-Martinez R.:
Departamento de Biología Celular, Facultad de Ciencias, Universidad Nacional Autónoma de Mexico, Mexico City, Mexico
Jimenez-Garcia L.F.:
Departamento de Biología Celular, Facultad de Ciencias, Universidad Nacional Autónoma de Mexico, Mexico City, Mexico
Camarena L.:
Departamento de Biología Molecular y Biotecnología, Instituto de Ivestigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico
Poggio S.:
Departamento de Biología Molecular y Biotecnología, Instituto de Ivestigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico
hybrid, All Open Access; Hybrid Gold
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