llecture 4 Flashcards
what does the signal peptidase recognise
small neutral side chains
what drives the movement across the ER
Sec63+BiP also HSP
ahs peptide binding domain and ATPases domain.
what does Sec63 promote
BiP-ATP hydrolysis. makes change so it can bind to polypeptide chain.
how does type 1 integral membrane protein insert into the membrane
hydrophobic TM domain enter translocon. the stop-transfer anchor sequence take place. once embedded translocation continues.
N-terminal ER sequence is cleaved. C-terminal is cytosilic
how is type 2 membrane protein inserted
located internally. SRP recognises it. TM domain is signal sequence. embeds in ER bilayer.
c-terminal is luminal
describe type 3 membrane insertion protein
same as type 2. positive charge placement is different on C-terminal side so C-terminus is in cytosol. has internal signal sequence can’t’ cleave.
give and example for type1,2,3
1= LDL receptor, insulin receptor, growth hormone receptor
2= transferin receptor
3= cytochrome 450
what do tail anchored membrane proteins depend on
Get3(ATPase) binds to c-terminal of protein. Get1/Get2 receptor recruits. ATP hydrolysis. c-terminus release and embedded
describe the topology of type 5 membrane protein
alpha helix direct, anchor or stop transfer protein to ER. N-terminus can be cytosolic or luminal.
what attaches phospholipid anchors to proteins
glycosylphosphatidylinositol which is a amphipathic molecule
what recognises the AA sequence near N-terminus
transamidase
what does transamidase do
cleave stop anchor sequence. transfer ER luminal part to GPI membrane anchor.
what modifications take place in the ER
N-linked glycosylation
disulphide bond formation
aid folding
oligomer formation
what modifications take place in the golgi
o-linked glycosylation
proteolytic processing
what modification takes place at the cell surface
protein shedding
describe how n-linked glycosylation takes place
glycan+ nitrogen atom of asparagine= oligosaccharide- nascent polypeptide in lumen of ER- cleave pyrophosphate bond between dolichol-glycan molecule. processing reactions. glucose and mannose removed. n-linked glycan- ER chaperones+ 3 glucose residues on core. help fold. 3 glucose removed. if fold fail + 3 glucose.
how do disulfide bonds form in secretory proteins
oxidising environment. link sulfhydryl groups. 2 cysteine residues. not in cytosolic protein. protein disulphide isomerase present. reducing agent. Ero 1- carries s-s bond to give to PDI. oxidise PDI. disulphides exchange on protein.
describe protein oligomer formation
spikes form hemagglutinin protein. trimers formed in ER of host cell. =precursor HA0.post translational.
what do o-glycosyltransferases do
+ activated sugars to O-atom on serine and threonine residues