GLORIA

GEOMAR Library Ocean Research Information Access

X

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Online Resource
    Online Resource
    In silico analysis of coevolution among ERMES proteins, Pex11, and Lam6
    Canadian Science Publishing ; 2017
    In:  Canadian Journal of Microbiology Vol. 63, No. 12 ( 2017-12), p. 984-997
    Details
    In: Canadian Journal of Microbiology, Canadian Science Publishing, Vol. 63, No. 12 ( 2017-12), p. 984-997
    Abstract: In eukaryotic cells, communication and dynamic interactions among different organelles are important for maintaining cellular homeostasis. The endoplasmic reticulum (ER) mitochondria encounter structure (ERMES) complex establishes membrane contact sites between ER and mitochondria and is essential for phospholipid transport, protein import, and mitochondrial dynamics and inheritance. In this work, in silico analyses were used to probe the intramolecular interactions in ERMES proteins and the interactions that support the ERMES complex. Based on mutual information (MI), sites of intramolecular coevolution are predicted in the core proteins Mmm1, Mdm10, Mdm12, Mdm34, the peroxisomal protein Pex11, and cytoplasmic Lam6; these sites are linked to structural features of the proteins. Intermolecular coevolution is predicted among the synaptotagmin-like mitochondrial lipid-binding protein (SMP) domains of Mmm1, Mdm12, and Mdm34. Segments of Pex11 and Lam6 also share MI with the SMP domains of Mmm1 and Mdm12 and with the N terminus of Mdm34, implicating Mdm34 as part of a hub for interactions between ERMES and other complexes. In contrast, evidence of limited intermolecular coevolution involving the outer membrane protein Mdm10 was detected only with Mmm1 and Pex11. The results support models for the organization of these interacting proteins and suggest roles for Pex11 and Lam6 in regulating complex formation.
    Type of Medium: Online Resource
    ISSN: 0008-4166 , 1480-3275
    URL: Article
    DOI: 10.1139/cjm-2017-0460
    RVK:
    WA 15000
    Language: English
    Publisher: Canadian Science Publishing
    Publication Date: 2017
    detail.hit.zdb_id: 280534-0
    detail.hit.zdb_id: 1481972-7
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 2
    Online Resource
    Online Resource
    Increased reactive oxygen species production and maintenance of membrane potential in VDAC-less Neurospora crassa mitochondria
    Springer Science and Business Media LLC ; 2019
    In:  Journal of Bioenergetics and Biomembranes Vol. 51, No. 5 ( 2019-10), p. 341-354
    Details
    In: Journal of Bioenergetics and Biomembranes, Springer Science and Business Media LLC, Vol. 51, No. 5 ( 2019-10), p. 341-354
    Type of Medium: Online Resource
    ISSN: 0145-479X , 1573-6881
    URL: Article
    DOI: 10.1007/s10863-019-09807-6
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2019
    detail.hit.zdb_id: 1482010-9
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 3
    Online Resource
    Online Resource
    Functional characterization of an N-terminally-truncated mitochondrial porin expressed in Neurospora crassa
    Canadian Science Publishing ; 2017
    In:  Canadian Journal of Microbiology Vol. 63, No. 8 ( 2017-08), p. 730-738
    Details
    In: Canadian Journal of Microbiology, Canadian Science Publishing, Vol. 63, No. 8 ( 2017-08), p. 730-738
    Abstract: Mitochondrial porin, which forms voltage-dependent anion-selective channels (VDAC) in the outer membrane, can be folded into a 19-β-stranded barrel. The N terminus of the protein is external to the barrel and contains α-helical structure. Targeted modifications of the N-terminal region have been assessed in artificial membranes, leading to different models for gating in vitro. However, the in vivo requirements for gating and the N-terminal segment of porin are less well-understood. Using Neurospora crassa porin as a model, the effects of a partial deletion of the N-terminal segment were investigated. The protein, ΔN2-12porin, is assembled into the outer membrane, albeit at lower levels than the wild-type protein. The resulting strain displays electron transport chain deficiencies, concomitant expression of alternative oxidase, and decreased growth rates. Nonetheless, its mitochondrial genome does not contain any significant mutations. Most of the genes that are expressed in high levels in porin-less N. crassa are expressed at levels similar to that of wild type or are slightly increased in ΔN2-12porin strains. Thus, although the N-terminal segment of VDAC is required for complete function in vivo, low levels of a protein lacking part of the N terminus are able to rescue some of the defects associated with the absence of porin.
    Type of Medium: Online Resource
    ISSN: 0008-4166 , 1480-3275
    URL: Article
    DOI: 10.1139/cjm-2016-0764
    RVK:
    WA 15000
    Language: English
    Publisher: Canadian Science Publishing
    Publication Date: 2017
    detail.hit.zdb_id: 280534-0
    detail.hit.zdb_id: 1481972-7
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 4
    Online Resource
    Online Resource
    The N-terminus of VDAC: Structure, mutational analysis, and a potential role in regulating barrel shape
    Elsevier BV ; 2016
    In:  Biochimica et Biophysica Acta (BBA) - Biomembranes Vol. 1858, No. 6 ( 2016-06), p. 1350-1361
    Details
    In: Biochimica et Biophysica Acta (BBA) - Biomembranes, Elsevier BV, Vol. 1858, No. 6 ( 2016-06), p. 1350-1361
    Type of Medium: Online Resource
    ISSN: 0005-2736
    URL: Article
    DOI: 10.1016/j.bbamem.2016.03.017
    RVK:
    WA 15000
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2016
    detail.hit.zdb_id: 2209384-9
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 5
    Online Resource
    Online Resource
    Proteomic Shifts Reflecting Oxidative Stress and Reduced Capacity for Protein Synthesis, and Alterations to Mitochondrial Membranes in Neurospora crassa Lacking VDAC
    MDPI AG ; 2022
    In:  Microorganisms Vol. 10, No. 2 ( 2022-01-18), p. 198-
    Details
    In: Microorganisms, MDPI AG, Vol. 10, No. 2 ( 2022-01-18), p. 198-
    Abstract: Voltage-dependent anion-selective channels (VDAC) maintain the bidirectional flow of small metabolites across the mitochondrial outer membrane and participate in the regulation of multiple cellular processes. To understand the roles of VDAC in cellular homeostasis, preliminary proteomic analyses of S100 cytosolic and mitochondria-enriched fractions from a VDAC-less Neurospora crassa strain (ΔPor-1) were performed. In the variant cells, less abundant proteins include subunits of translation initiation factor eIF-2, enzymes in the shikimate pathway leading to precursors of aromatic amino acids, and enzymes involved in sulfate assimilation and in the synthesis of methionine, cysteine, alanine, serine, and threonine. In contrast, some of the more abundant proteins are involved in electron flow, such as the α subunit of the electron transfer flavoprotein and lactate dehydrogenase, which is involved in one pathway leading to pyruvate synthesis. Increased levels of catalase and catalase activity support predicted increased levels of oxidative stress in ΔPor-1 cells, and higher levels of protein disulfide isomerase suggest activation of the unfolded protein response in the endoplasmic reticulum. ΔPor-1 cells are cold-sensitive, which led us to investigate the impact of the absence of VDAC on several mitochondrial membrane characteristics. Mitochondrial membranes in ΔPor-1 are more fluid than those of wild-type cells, the ratio of C18:1 to C18:3n3 acyl chains is reduced, and ergosterol levels are lower. In summary, these initial results indicate that VDAC-less N. crassa cells are characterized by a lower abundance of proteins involved in amino acid and protein synthesis and by increases in some associated with pyruvate metabolism and stress responses. Membrane lipids and hyphal morphology are also impacted by the absence of VDAC.
    Type of Medium: Online Resource
    ISSN: 2076-2607
    URL: Article
    DOI: 10.3390/microorganisms10020198
    Language: English
    Publisher: MDPI AG
    Publication Date: 2022
    detail.hit.zdb_id: 2720891-6
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...