Chapter 8; protein localization
Terms
undefined, object
copy deck
- RNA
- The major substrate for nuclear export is [protein, RNA, importins]
- di
- Importin alpha-beta is a(n) [n]mer.
- 120
- The overall diameter of the nuclear pore structure (not the pore itself) is approximately [n] nm in diameter.
- 10; leucine
- The nuclear export sequence (NES) consists of a [n] amino acid sequence featuring a pattern of conserved [amino acid].
- is not
- The addition of a single ubiquitin unit [is, is not] sufficient to trigger degradation by the proteasome.
- yes
- Do the SRP and SRP receptor BOTH have GTPase activity?
- phobic
- Protein folding is driven by the aggregation of hydro....... sequences.
- 40
- Motifs which bind to the Hsp70 chaperone occur approximately every [number] amino acids.
- direction of transport
- Ran is important in the control of [transport receptor specificity, direction of transport, opening and closing of nuclear pores].
- GTP
- Nuclear export complexes are stabilized by the [GTP, GDP]-bound form of Ran.
- E3
- Specificity of ubiquitination usually depends on selectivity of the [E1, E2, E3] species.
- alpha helix; amphipathic
- The organelle protein leader sequence forms a [secondary structure] which is [basic, amphipathic, acidic, hydrophillic].
- Sec61
- The segment of the translocon which interacts with the ribosome to form a seal during translocation is [name of subunit]
- positive
- Regions at the margins of internal signal-anchor sequences carry [positive or negative] charges.
- KDEL; C
- Proteins targeted to the ER contain the sequence [tetrapeptide sequence] at their [N or C] terminal.
- cross
- Chloroplast proteins targeted to locations within the thyalkoid lumen [cross, do not cross] the stroma en route.
- signal recognition particle
- Attachment of a translating ribosome to the ER requires the protein [protein name; not an acronym]
- both directions
- Nuclear transport occurs in [one direction, both directions].
- 20; 26
- The archaeal proteasome exists in a smaller [n]S form and a larger [n]S form.
- E3
- Elongation of the ubiquitin chain is carried out by [E1, E2, E3].
- yes
- Can a single protein feature both an NES and an NLS?
- E2; E1; E2
- [E1, E2, E3] is referred to as the ubiquitin-conjugating protein; it transfers ubiquitin from [E1, E2, E3] to [E1, E2, E3, the substrate protein].
- chaperones
- Proteins which cannot renature into an active conformation require:
- are
- The three classes of RNA [are, are not] each transported by their own system of proteins.
- transport receptor
- The analog of the SRP in nuclear import is the [protein name]; it binds both the nuclear pore and the cargo protein.
- N
- In group I transmembrane proteins, the [N or C] terminus faces the extracellular space.
- E3, E2
- [E1, E2, E3], or ubiquitin ligase, transfers ubiquitin from [E1, E2, E3] to the substrate protein.
- proline
- The amino acid [name of amino acid] is often located in the upstream portion of the NLS.
- internal
- Group II transmembrane proteins have a(n) [terminal, internal] signal sequence.
- self-assembly
- The ability of a denatured protein to renature into an active form is called:
- true
- The nuclear localization sequence is unconserved. True or false?
- can
- Nuclear export or import by a specific pathway [can, cannot] be saturated.
- cotranslational
- Translocation in which a nascent protein associates with the translocation apparatus while still attached to the ribosome
- translocation
- The process of inserting a protein into or passing a protein through a membrane:
- shuttle between nucleus and cytosol
- Poly-a tail binding proteins [remain in the cytosol, remain in the nucleus, shuttle between nucleus and cytosol].
- occluded; open
- The eukaryotic proteasome's center [open, occluded]; the archaeal proteasome's center is [open, occluded].
- different from
- In the eukaryotic proteasome, all alpha and all beta subunits are [the same as, different from] all others.
- cytoplasmic
- More positively charged residues are found on the residues on the [cytoplasmic or luminal] side of the anchor.
- 76; covalent bond
- Ubiquitin is a [n]-residue long protein which is linked to substrates by a(n) [ionic interaction, covalent bond, disulfide bridge].
- philic; phobic
- The surface of a protein is generally hydro........; the lipid core of a membrane is hydro........
- E1
- The ubiquitin-activating protein [E1, E2, E3] links itself to ubiquitin.
- acidic, basic
- The organelle targeting sequence contains both [acidic,uncharged] and [basic, aromatic, modified] amino acids.
- GDP
- Nuclear import complexes are stabilized by the [GTP, GDP]-bound form of Ran.
- 70
- The translocon pore is closed/sealed until the peptide is [n] amino acids in length.
- lysosome
- Ubiquitinated plasma-membrane proteins are degraded by the [name of agent].
- true
- All protein is synthesized in the cytosol, and all RNA is synthesized in the nucleus. True or false?
- Pex5p
- Peroxisome proteins bearing the sequence designated PTS1 are imported with the help of [protein name].
- CAS
- Importin alpha, when located in the nucleus, is bound by [protein name], which functions as an exportin.
- Hsp90
- ....... is a chaperone protein involved in signal transduction (i.e. steroid receptors and signaling kinases).
- N
- Cotranslationally translocated peptides are generally targeted by [N or C] terminal sequences.
- SRP; SRP receptor
- Attachment of a translating ribosome begins with recognition of the signal sequence by the [protein], which binds to the membrane-associated protein [protein name].
- 46, lys
- Subsequent ubiquitins are linked to the chain at position [n], which is the amino acid [3-letter code].
- are not
- All NLS sequences [are, are not] composed of a single, uninterrupted stretch of basic amino acids.
- yes
- Do combined signal-anchor sequences resemble cleavable signal sequences?
- nuclear pore; cargo NLS
- Importin alpha-beta's beta subunit binds to the [nuclear pore, cargo NLS], while its alpa subunit binds to the [nuclear pore, cargo NLS].
- signal peptidase
- The [name of protein] cleaves the signal sequence from the peptide after translocation.
- 7; or
- Each of the proteasome's four 'rings' consists of [n] alpha [and, or] beta subunits.
- N
- In group II transmembrane proteins, the [N or C] terminus faces the cytoplasm.
- eight
- The nuclear pore consists of inner and outer ring structure with [n]fold symmetry.
- 10
- The actual pore created by the nuclear pore is [n] nm in diameter
- 15 to 30; phobic
- Cotranslational insertion is directed by a signal sequence which is [range of numbers] amino acids, consisting largely of hydro[phillic or phobic] amino acids.
- anchor
- In Group II transmembrane proteins, the singal sequence is combined with a(n) ......... sequence.
- single proteins
- The transport receptors importin-beta3 and transportin are [single proteins; multi-subunit complexes].
- 3 to 4; C
- The signal for transport to the peroxisome is [number] amino acids long, and located at the [N or C] terminus.
- 25
- Mitochondrial and chloroplast proteins are targeted to their respective membranes with [~number] amino acid sequences.
- 4 to 9; basic
- The nuclear localization signal is [number] amino acids long; it is composed of [electronic character] amino acids.
- anchoring in the membrane
- The eight 'arms' of the nuclear pore may be responsible for [anchoring in the membrane, other options]
- GDP; GAP
- Ran-[GTP, GDP] is found in the cytosol, due to the activity of [GEF, GAP].
- 12
- Ion channels typically have [number] alpha-helical transmembrane domains.
- GTP; GEF
- Ran-[GTP, GDP] is found in the nucleus, due to the activity of [GEF, GAP].
- beta
- The [alpha, beta, alpha and beta] subunits of the archaeal proteasome have protease activity.
- Chaperonin
- Unlike the Hsp70 system, the ............. system consists of a large oligomeric "cage" which provides an environment conducive to correct folding.
- short, basic
- The nuclear localization sequence is [short, long] and contains [basic, acidic, aliphatic] residues
- cap-binding complex
- The export protein active for snRNAs is the [protein name]
- no
- Are ribosomes attached to the rough ER a distinct species from those operating in the cytosol?
- the same
- The nucleus and the cytoplasm are separated by nuclear pores, which help to maintain the nucleus and cytosol in [the same, different] ionic conditions.
- false
- The cotranslational targeting sequence is retained in the mature protein. True or false?
- Sec61; tri
- The translocon's pore is formed by the subunit [name of peptide]; it is a(n) [n]mer.
- plasma membrane
- The 'default' sorting pathway ultimately leads to the:
- GroEL/GroES; TRiC
- The two chaperonin systems are [present in all organisms] and [present in the eukaryotic cytosol].
- beta
- Single-protein transport receptors most resemble the [alpha, beta] subunit of importin alpha-beta.
- true
- Misfolded proteins can be ejected from the ER to be degraded in the cytoplasm. True or false?
- false
- True or false: the organelle targeting sequence is highly conserved across all eukaryotic organisms.
- Hsp40; GrpE
- The components of the Hsp70 system are Hsp70, ........ and ......
- matrix
- The default destination for mitochondrial proteins is the [outer membrane, intermembrane, matrix, inner membrane].
- BiP
- [name of protein] acts as a molecular ratchet on the luminal side of translocon, preventing the nascent polypeptide from 'slipping' backwards.
- open; closed
- The translocon is an aqueous channel through the ER membrane; before ribosome binding, it is [open/closed] at the cytosolic face and [open/closed] at the luminal face.
- 7
- G-protein coupled receptors have [number] transmembrane domains.
- unconserved
- The nuclear localization sequence is [conserved, unconserved].
- cytosol, folded
- Once Pex5p or Pex7p is bound to a peroxisome-targeted protein located in the [cytosol, ER], the protein is imported into the peroxisome in its [folded, unfolded] conformation.
- opposite
- An odd number of membrane-spanning domains implies that the N and C termini face the [same, opposite] side(s) of the membrane.
- cleavage, is
- The mitochondrial leader sequence is modified by [prenylation, acylation, phosphorylation, cleavage, association with chaperone proteins] if the protein [is, is not] intended for a location other than the matrix.
- true
- Chaperones are responsible for maintaining proteins in an unfolded state prior to transport. True or false?
- requires; requires
- Nuclear import [requires, does not require] a carrier protein; nuclear export [requires, does not require] a carrier protein.
- mannose-6-phosphate
- Proteins targeted to the lysozome have a [molecule] tag.
- Pex7p
- Peroxisome proteins bearing the sequence designated PTS2 are imported with the help of [protein name].