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PEROXISOMES

All of their proteins are encoded in the nucleus


Selective import from the cytosol
OXIDATIVE ENZYMES, catalase and urate oxidase
-> crystalloid core

Major sites of oxygen utilization
Oxidation reaction that produces hydrogen peroxide (H2O2)
RH2 +O2 -> R+H2O2
CATALASE uses the H2O2 H2O2 + RH2 -> R + 2H2O.

DETOXIFY various toxic molecules
25% of the ethanol we drink is oxidized to acetaldehyde



catalase converts excess H2O2 to H2O
2H2O2 -> 2H2O + O2

BREAKDOWN OF FATTY ACID MOLECULES,
oxidation shortens the alkyl chains of fatty acids sequentially in blocks of
two carbon atoms at a time, thereby converting the fatty acids to acetyl CoA



PLASMALOGENS, most abundant class of phospholipids in MYELIN (12-31)

peroxisomal disorders lead to neurological disease, Plasmalogen deficiencies
Zellweger syndrome, in which a defect in importing proteins -> peroxisomal
deficiency
Severe abnormalities in their brain, liver, and kidneys, and they die soon after birth

mutation in the gene encoding peroxin Pex2

defective receptor for the N- terminal import signal



SS: three amino acids (SerLysLeu) located at the C-terminus, import signal
Soluble receptor proteins in the cytosol, which recognize the targeting signals, and
docking proteins on the cytosolic surface (peroxins)

Import resemble protein transport into the nucleus (folded and oligomeric prots)



ER

> than half of the total membrane
ER lumen, more than 10% of the total cell volume
lipid and protein biosynthesis
cells organelles, ER, Golgi apparatus, lysosomes, endosomes, secretory
vesicles, plasma membrane
lipids for mitochondrial and peroxisomal membranes
proteins secreted @ exteriorlumen of the ER, Golgi apparatus, or lysosomes

Protien import is a co-translational
Ribosome attached directly to the ER membrane
ROUGH ER
SMOOTH ER
HEPATOCYTE, also has abundant smooth ER.
principal site of production of lipoprotein particles, which carry lipids via the
bloodstream,
enzymes synthesize lipid components of the particles
detoxification reactions are carried out by the cytochrome P450 enzymes

INTRACELLULAR CA2+ STORE
Ca2+ pump transports Ca2+ from the cytosol into the ER lumen
High concentration of Ca2+-binding proteins

MICROSOMES
small authentic versions of the ER,
protein translocation, protein glycosylation, Ca2+ uptake and release, and
lipid synthesis (12-37)

ER captures selected proteins from the cytosol (12-38)
transmembrane proteins
water-soluble proteins
directed to the ER membrane by an ER signal sequence
N-terminal leader peptide, signal peptidase
signal-recognition particle (SRP), SRP receptor
halts protein synthesis when signal peptide has emerged from the ribosome

bind to the ER membrane before completion of the polypeptide chain


secreted and lyso-somal hydrolases -> wreak havoc in the cytosol
chaperone proteins are not required to keep the protein unfolded

2 spatially separate populations of ribosomes
FREE RIBOSOMES, Membrane-bound ribosomes, a polyribosome
(12-40)
core of the translocator, called the Sec61 complex
aqueous pore (gated, Ca+2 block) and lateral opening to lipid (21-43)

(12-44)

START/STOP TRANSFER SIGNALS
Single pass, multiple pass, secreted proteins

Membrane proteins always inserted from the cytosolic side of ER
All copies of the same polypeptide will have the same orientation in the lipid
bilayer.
Asymmetrical ER membrane
This asymmetry is maintained during membrane budding and fusion events

ER resident proteins contain an ER RETENTION SIGNAL AA at their C-terminus
ER resident protein is protein disulfide isomerase (PDI)
SH on cysteines


Cysteines exposed to either the extracellular space or the lumen in the secretory and
endocytic pathways are disulfide-bonded
ER resident protein is the chaperone protein BiP
BiP recognizes incorrectly folded proteins (Hsp70 family), ATPase

Covalent addition of sugars to proteins, glycoproteins (N-linked)
-> Golgi apparatus, lysosomes, plasma membrane, or extracellular space
ER chaperone proteins, calnexin and calreticulin require Ca2+ (LECTINS)
Sugars help achieve properly folded or oligomeric state.
Misfolded proteins are exported from the ER back into the cytosol, degraded

ER enzymes, attach a glycosylphosphatidyl-inositol (GPI) anchor to the C-
terminus of some membrane proteins destined for the plasma membrane

glycosylation all of the major classes of lipids, phospholipids and cholesterol,
required for the production of new cell membranes Mbr synthesis

Phospholipid synthesis in the cytosolic half of the ER lipid bilayer


Phospholipid translocator called a scramblase, which equilibrates phospholipids
between the two leaflets of the lipid bilayer
flippases specifically remove phospholipids containing in their head groups free
amino groups (phosphatidylserine and phosphatidylethanolaminefrom the
extracellular leaflet and use the energy of ATP hydrolysis to flip them directionally
into the leaflet facing the cytosol

ER also produces cholesterol and ceramide
Ceramide is exported to the Golgi apparatus
glycosphingolipids, sphingomyelin