Organelles 2 Flashcards
Which end is ERSS found on? A. C-terminus B. 5' of MRNA C. 3' of Coding Strand D. 5' of Template Strand
B. 5' Of MRNA this is seen because the 5'-3' Coding 3'-5' Template 5'-3' MRNA N-Terminus- C-Terminus
Where does thing binding happen in the cell of the ERSS to SRP?
Cytosol.
There is an infuffiency within the enzyme signal Peptidase. This occurred because of a missense mutation where a glutamic acid was entered instead of leucine at position 342. An enhancer was noted for the gene coding for ubiquitin activating enzyme. Explain the occurrence of miss folded proteins?
A. Increased negative charge due to Glutamic acid
B. Disruption of polarity
C. Inability to fold the incoming protein
D. Increased hydrophilic effects
C. Inability to fold the incoming protein
This may seem obscure because there is a distinction. Here we know that there SRP binds to the Hydrophobic Amino Acids within the ERSS. The same goes for the Signal Peptidase. if there is subsitution of an charged amino acid within the structure the signal peptidase. therefore the signal peptidase can no longer have interactions with the hydrophobic interactions with ERSS. Therefore it can not cleave the sequence therefore hindering the folding of protein. Causing an increase of ERAD pathway for degradation.
Serving as many Regulatory Steps within the RER Co-Translational Translocation in which GTP is hydrolyzed to by the SRP receptor, in which is it is then deasscoaited from the Complex. Therefore beginning translation into the lumen of the ER. Cleaving the signal sequence and allowing for the Stop transfer anchor sequence to take halt. A secondary Process occurs increasing the water solubility and affinity. Which Amino acid is particlar to this process? A. Tyrosine B. Threonine C. Serine D. Phenylalanine E. Aspasragine
Glycosylation begins in the ER and several sugars are put on to a dolichol Carrier which is then put on to a Aspargine residue.
The Responsible enzymes for the previous vignette is A. Peptidyl Transferase B. N-Linked Glycotransferase C. Oligiosacchride Protein Transferase D. Monoamine Oxidase
C. Oligiosacchride transferase
Your 3 years old female patient present with salty skin, increased chloride, thick mucous secretion within the lungs, she present with rhonchi, and positive rales within. A malformation of one of the reabsorption protein where misfolded, and sent for degradation. However proteins do undergo several rounds of folding and addition of several oligiosacchrides to aid within the folding process. Upon inspection of the protein within the lab, the leucine, proline, isoleucine Amino Acid residues where noted on the exterior of the protein. Which protein is responsible? A. Calreticulin B. Calenexin C. Protein Disulfide Isomerase D. Binding Immunoglobulin Protein
D. Binding Immunoglobulin Protein- is respsobsible for shielding and folding hydrophobic portions of a polypeptide to the folded protein interior (ATP- Dependent Process)
Upon looking at the DNA sequence of a protein it was noted there were more hydrogen bonds present within the helical structure. As a result while appreciating the amino acid sequence within the lumen several reaction were noted, one being strong interaction occured stabailizing the folding of this protein. Which interaction are responsible for the protein stabilization? A. Cystine- Guanine B. Cysteine- Cysteine C. Adenine- Uracil D. Guanine- Thyamine
B. Cysteine- Cysteine- Known for creating Strong Disulfide Bridges. . Protein Disulfide Isomerase facilitates this process
Once glycosylation has complete there, exiting the RER, will not enter into the Cis face of the Golgi through vesicle budding from the ER. This process is specific enough where if there isn’t a specific molecule the ER membrane will begin the budding process despite the transmembrane cargo protein and the Coat.
Which molecule is responsible for this change in the membrane?
A. Guanine Nucleotide Exchange Factor
B. Small GTP Binding Factor
C. Coat Adapter
D. Soluble Cargo Protein
D. Soluble Cargo Protein
If You got this wrong listen to the lecture capture.
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Dissociation of the vesicle coat is vital for the the endocytotic function of the vesicle. Seen within the pathology. XXYG, there is no dissociation of the vesicle. As a result of this which step is haltered and which protein is responsible it?
A. Vesicle Tethering - V-Snare
B. Vesicle Fusion- RAB GTP
C. Vesicle Tethering- T-Snare
D. Vesicle Tethering RAB GTP
E. Vesicle Fusion - Transmembrane Cargo Protein
F. Vesicle Fusion- Snare Pair
D. Vesicle Tethering RAB GTP
Lysosomal Enzymes are also known as acid hydrolyses enzymes known as peptidase, nuclease, lipase, etc. These enzymes are put sent through the secretory pathway, via ERSS. Ultimately entering Anterograde Vesiclar transport. However a Error was found within the tran face of the Golgi. The enzyme must be sent over to the RER. For further chaperon functions. Which mechanism is most responsible for reaching the ER? A. COP1 B.COP2 C. Soluble Cargo D. Ub-Ligase
Retrograde Transport is being described here therefore COP1 is responsible
What is the function of the ERSS?
it Functions to bind the SRP?
Function of the SRP?
Signal Recognition Peptide is function to mediate transport of the MRNA, Ribosome, Polypeptide to the Membrane of the Rough Endoplasmic Ret.
