23. Normal,
isolated liver
mitochondrion
Liver mitochondrion
treated with a protein
(tBID) that induces
programmed cell death
or apoptosis
• Mitocondria de hígado normal
• Mitocondria de hígado en apoptosis
• Mitocondria de un paciente con enfermedad mitocondrial
26. 1. Un fagotrofo fagocita a su presa.
2. Emergen individuos en la población de presas que son resistentes a
ser digeridas
3. Emerge una relación simbiótica facultativa entre el fagotrofo y la presa
4. Cambio de endosimbionte facultativo a endosimbionte obligado
5. El endosimbionte obligado evoluciona y se convierte en organelo
(mitocondria)
53. Mitochondrion from
chicken cerebellum
Hydrogenosomes from
the anaerobic fungus
Neocallimastix patriciarum
Hydrogenosomes from
the cattle parasite
Tritrichomonas foetus
Mitosomes from the
intestinal parasite
Entamoeba histolytica,
Mitosomes from the
the microsporidian
Trachipleistophora
hominis
Mitosomes from the
diplomonad Giardia
intestinalis
58. cox 3
Cuando un gen migra de la mitocondria al núcleo……
¿Qué sucede?
¿Qué hemos aprendido?
59. cox 3
Adquirió una región que codifica para una
presecuencia mitocondrial……
N
+ +++ + - ++
- -
+ + +
100 – 140 residuos que forman alfa-
hélices anfipáticas
Fig. 3. Cryo-EM tomogram of a crista junction in Saccharomyces cerevisiae. (A) Single slice through a tomogram of an isolated vitrified wild type mitochondrion from S. cerevisiae. (B) Magnified view of boxed area in left panel. (C) Surface rendered view of a crista junction. Scale bars 100 nm. EM tomogram with courtesy of Dr Marek Cyrklaff.
Fig. 4. Subcompartmentalization of the mitochondrial inner membrane. The distribution of mitochondrial proteins involved in several major processes of mitochondria has been determined by quantitative immunoelectron microscopy in S. cerevisiae [50]. Inner membrane proteins involved in mitochondrial fusion (Mgm1p) or protein translocation (Mia40p, TIM23 complex) are preferentially located in the inner boundary membrane. In contrast, proteins involved in oxidative phosphorylation (ANC, Complex III, Complex IV, F1FO-ATP synthase) and in iron/sulfur cluster biogenesis (Fe/S cluster) are enriched in the cristae membrane. This distribution is uneven, yet not exclusive nor static. Proteins dynamically redistribute between the domains depending on the physiological state of the cell. CS, Cytosol; OM, outer membrane; IMS, intermembrane space; IM, inner membrane; M, matrix space. Style adapted from the illustrations of Graham T. Johson in [203].
Changes in internal organization of mitochondria associated with cell death and disease: (A) Normal, isolated liver mitochondrion (Mannella et al., 2001), (B) Liver mitochondrion treated with a protein (tBID) that induces programmed cell death or apoptosis (Scorrano et al., 2002), and (C) Mitochondrion from a patient with a mitochondrial myopathy (M. Huizing, 1998, PhD Thesis, Univ. Nijmegen).
Evolution of the Molecular Machines for Protein Import into Mitochondria
Fig. 2. The protein import machinery in mitochondria of the yeast S. cerevisiae. Arrows indicate the directional flow of protein substrates from their site of synthesis in the cytosol to each of the submitochondrial compartments. Subunits of the protein import machinery have been color-coded: Those with functional homologs in bacteria are in black, and the eukaryote-specific core components of the TOM and TIM machinery are in color. Shaded gray are components of the import machinery that are only found in fungi and animals, which suggests that they might be modules added to the machinery relatively recently. Stars depict the essential yeast proteins.