Shuvo 2017 Can J Microbiol

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Publications in the MiPMap
Shuvo SR, Kovaltchouk U, Zubaer A, Kumar A, Summers WAT, Donald LJ, Hausner G, Court DA (2017) Functional characterization of an N-terminally-truncated mitochondrial porin expressed in Neurospora crassa. Can J Microbiol 17:1-9.

Β» PMID: 28414919

Shuvo SR, Kovaltchouk U, Zubaer A, Kumar A, Summers WAT, Donald LJ, Hausner G, Court DA (2017) Can J Microbiol

Abstract: Mitochondrial porin, which forms voltage-dependent anion-selective channels (VDAC) in the outer membrane, can be folded into a 19-Ξ²-stranded barrel. The N terminus of the protein is external to the barrel and contains Ξ±-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, Ξ”N2-12porin, 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 Ξ”N2-12porin 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. β€’ Keywords: Mitochondrial porin, VDAC, N-terminus, Neurospora crassa, Alternative oxidase β€’ Bioblast editor: Kandolf G

Labels: MiParea: Respiration, mtDNA;mt-genetics, Genetic knockout;overexpression 

Organism: Fungi 

Preparation: Isolated mitochondria 

Coupling state: ROUTINE 

HRR: Oxygraph-2k 


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