1.7 - Sub-cellular organelles – Bioch + OB Flashcards

1
Q

structure + function of the cell membrane

A

see other topic

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1
Q

size of the cell membrane

A

5-7nm

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2
Q

structure of the rER

A

Dotted with ribosomes – dotted appearance

membrane is continuous with the outer membrane of the nuclear envelope = facilitating efficient transport of mRNA from the nucleus to ribosomes for translation.

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3
Q

function of the rER

A

Site of protein synthesis – matured mRNA fragments being shipped into this region through nuclear envelopes

Used as a template for translation

N-linked glycosylation also takes place here in glycoprotein formation

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4
Q

structure of the sER

A

Found more freely in cytoplasm + lacks ribosomes

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5
Q

function of the sER

A

Responsible for synthesis of lipids / phospholipids / sterols – typically following lipid processing or lipogenesis

ER plays a crucial role in detoxifying drugs and harmful metabolites

storage site for calcium

Well-developed sER = muscular sarcoplasmic reticulum, from which Ca2+ levels are regulated in response to signals at the NMJ

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6
Q

structure of ribsomes

A

Small proteins combined with rRNAs

80s in eukaryotes

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7
Q

function of ribosomes

A

Site of translation of mRNA to a primary sequence = uses tRNA to align appropriate amino acids + condense them to form peptide bonds

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8
Q

structure of golgi apparatus

A

Does not touch
Found in cytosol
cis + trans face

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9
Q

function of the golgi apparatus

A

primary role = package extracellular proteins in vesicles as they move from the cis to trans face = allows for more effective movement to the plasmalemma for endocytosis + secretion

protein modification - glycosylation + phosphorylation= provides post-translational modifications

produces lysosomes

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10
Q

structure of mitochondria

A

Double Membrane:
Outer Membrane
Inner Membrane - Highly folded into cristae, which increase surface area for biochemical reactions; impermeable to ions and small molecules.

Intermembrane Space: The space between the outer and inner membranes, involved in creating a proton gradient.

Matrix: The innermost compartment containing enzymes for the citric acid cycle, mitochondrial DNA, ribosomes, and metabolic substrates.

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11
Q

function of mitochondria

A

ATP production
anabolic functions
amino acid metabolism
ca2+ homeostasis with ER
lipid synthesis

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12
Q

significance of exposure to the internal membrane of mitochondria

A

exposure to internal membrane can promote the rest of the cell to initiate the caspase-9 mediated cell apoptosis pathway

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13
Q

why dont all cells have mitochondria

A

not all cells have these organelles as they require an oxygen-rich environment for normal function – RBCs

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14
Q

structure of lysosomes

A

enclosed by single lipid bilayer

contain a variety of digestive enzymes (hydrolases) = proteases, lipases, nucleases, carbohydrases. = function optimally at acidic pH 4.5-5

maintained that pumps in the membrane that transport H⁺ ions into the organelle

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15
Q

function of lysosomes

A

break down damaged proteins / organelles / pathogens within cell

endocytosis
phagocytosis
autophagy
apoptosis

reply on strong cell membrane and closely controlled H+ transportation = to flood lumen of the organelle with protons + hydrolytic enzymes of lysozyme family = then breaks down anything caught inside it

16
Q

what is autophagy

A

degrade damaged organelles and recycle their components

17
Q

structure of endosome

A

specific vesicles produced by the Golgi apparatus

18
Q

function of endosome

A

sorting of endocytosed material -Some materials (like receptors) are recycled back to the plasma membrane, while others (like ligands) are sent to late endosomes for eventual degradation in lysosomes

shuttle molecules between the plasma membrane, lysosomes, and the trans-Golgi network

19
Q

structure of peroxisome

A

single membrane

matrix = contains a variety of oxidative enzymes, such as catalase, urate oxidase, and D-amino acid oxidase.

in cytoplasm

20
Q

function of peroxisome

A

Proteins destined for peroxisomes are synthesised in the cytosol + contain a specific sequence known as a peroxisomal targeting signal

involved in the β-oxidation of very long-chain fatty acids (VLCFAs)

fatty acids are shortened in the peroxisome + then further processed in mitochondria to produce energy (ATP).

peroxisomal β-oxidation does not directly contribute to ATP production = but generates hydrogen peroxide as a byproduct

breaking down hydrogen peroxide = harmful byproduct of oxidative reaction = into water and oxygen using the enzyme catalase.

neutralise ROS

21
Q

three major parts of the cytoskeleton

A

microtubules

intermediate fibres

actin

22
Q

structure of microtubules

A

polymers of the protein tubulin

consist of alpha and beta tubulin = forms heterodimers

heterodimers polymerise into protofilaments

one microtubule is made from 13 protofilaments

slightly staggered

23
Q

how many protofilaments make one microtubule

A

13

24
Q

why are microtubules slightly staggered

A

because of the two types of contact - vertical and lateral contact

two protofilaments not completely parallel in lateral contact= shifted along z axis

important in the dynamic microtubule lattice

25
Q

whats the difference between alpha and beta tubulin

A

both bind to GTP

beta tubulin can hydrolyse GTP to GDP alpha can not

26
Q

what happens when beta tubulin hydrolyses GTP into GDP

A

changes its conformation from T form to D form

now D form doesnt really fit staggered conformation

so leads to the depolymerisation of protofilaments

27
Q

what is dynamic instability

A

GTP and beta tubulin is loaded onto the growing plus ends of microtubules = GTP cap

as long as hydrolysis not outpace the assembly rate (addition of more GTP loaded subunits) = microtubules grow

if hydrolysis rate greater then assembly = catastrophe

if rate of assembly greater = recovery

28
Q

plus and minus end of microtubules

A

Plus end = rapidly built and destabilised

Minus end = near the nucleus, stabilised

29
Q

define catastrophe and recovery

A
30
Q

importance of dynamic instability

A

depolymerisation can be used to create force - e.g. chromosomes attached to microtubules are removed by catastrophic depolymerisation

31
Q

What are MAPs, and how do they regulate microtubule dynamics?

A

Microtubule-Associated proteins

interact with microtubules

  • promote microtubule polymerisation and prevent excess depolymerisation
  • modulate the rate of microtubule growth and shrinkage by binding to tubulin subunits or the MT lattice
  • help organise MT into bundles + networks
31
Q

example of MAPs

A

Tau:
Found in neurons, Tau stabilizes microtubules in axons.

Pathological aggregation of Tau is linked to neurodegenerative diseases like Alzheimer’s.

32
Q

what is gamma tubulin

A

nucleates microtubules at microtubule organising center = associated with minus end

33
Q

polarity of MTs

A

cell specific

important for the directionality of transport - moving organelles around the cell