scholarly journals Organelle Division and Cytoplasmic Inheritance

BioScience ◽  
1996 ◽  
Vol 46 (11) ◽  
pp. 827-835 ◽  
Author(s):  
Tsuneyoshi Kuroiwa ◽  
Hidenobu Uchida
1998 ◽  
Vol 8 (17) ◽  
pp. R619-R621 ◽  
Author(s):  
Joe Lutkenhaus
Keyword(s):  

1999 ◽  
Vol 18 (1) ◽  
pp. 7-10 ◽  
Author(s):  
Barbara Reyna ◽  
Rita Pickler

Neonatal nurses need to understand the basic patterns of genetic transmission. This article, the first in a series, provides an overview of Mendel’s laws and discusses five types of transmission: single gene inheritance, chromosomal inheritance, multifactorial inheritance, cytoplasmic inheritance, and somatic cell mutations.


2020 ◽  
Author(s):  
Josiah B. Passmore ◽  
Ruth E. Carmichael ◽  
Tina A. Schrader ◽  
Luis F. Godinho ◽  
Sacha Ferdinandusse ◽  
...  

AbstractPeroxisomes are highly dynamic subcellular compartments with important functions in lipid and ROS metabolism. Impaired peroxisomal function can lead to severe metabolic disorders with developmental defects and neurological abnormalities. Recently, a new group of disorders has been identified, characterised by defects in the membrane dynamics and division of peroxisomes rather than by loss of metabolic functions. However, the contribution of impaired peroxisome plasticity to the pathophysiology of those disorders is not well understood. Mitochondrial fission factor (MFF) is a key component of both the peroxisomal and mitochondrial division machinery. Patients with MFF deficiency present with developmental and neurological abnormalities. Peroxisomes (and mitochondria) in patient fibroblasts are highly elongated as a result of impaired organelle division. The majority of studies into MFF-deficiency have focused on mitochondrial dysfunction, but the contribution of peroxisomal alterations to the pathophysiology is largely unknown. Here, we show that MFF deficiency does not cause alterations to overall peroxisomal biochemical function. However, loss of MFF results in reduced import-competency of the peroxisomal compartment and leads to the accumulation of pre-peroxisomal membrane structures. We show that peroxisomes in MFF-deficient cells display alterations in peroxisomal redox state and intra-peroxisomal pH. Removal of elongated peroxisomes through induction of autophagic processes is not impaired. A mathematical model describing key processes involved in peroxisome dynamics sheds further light into the physical processes disturbed in MFF-deficient cells. The consequences of our findings for the pathophysiology of MFF-deficiency and related disorders with impaired peroxisome plasticity are discussed.


1972 ◽  
Vol 29 (2) ◽  
pp. 152-161 ◽  
Author(s):  
Igor B. Dawid ◽  
Antonie W. Blackler

PROTOPLASMA ◽  
2020 ◽  
Vol 258 (1) ◽  
pp. 19-32
Author(s):  
Yuan Shen ◽  
Toyoki Iwao ◽  
Taizo Motomura ◽  
Chikako Nagasato

1996 ◽  
Vol 135 (1) ◽  
pp. 123-137 ◽  
Author(s):  
P A Marshall ◽  
J M Dyer ◽  
M E Quick ◽  
J M Goodman

Pex11p (formerly Pmp27) has been implicated in peroxisomal proliferation (Erdmann, R., and G. Blobel. 1995. J. Cell Biol. 128; 509-523; Marshall, P.A., Y.I. Krimkevich, R.H. Lark, J.M. Dyer, M. Veenhuis, and J.M. Goodman, 1995. J. Cell Biol. 129; 345-355). In its absence, peroxisomes in Saccharomyces cerevisiae fail to proliferate in response to oleic acid; instead, one or two large peroxisomes are formed. Conversely, overproduction of Pex11p causes an increase in peroxisomal number. In this report, we confirm the function of Pex11p in organelle proliferation by demonstrating that this protein can cause fragmentation in vivo of large peroxisomes into smaller organelles. Pex11p is on the inner surface of the peroxisomal membrane. It can form homodimers, and this species is more abundant in mature peroxisomes than in proliferating organelles. Removing one of the three cysteines in the protein inhibits homodimerization. This cysteine 3-->alanine mutation leads to an increase in number and a decrease in peroxisomal density, compared with the wild-type protein, in response to oleic acid. We propose that the active species is the "monomeric" form, and that the increasing oxidative metabolism within maturing peroxisomes causes dimer formation and inhibition of further organelle division.


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