Translation and Proteins - GRE Subject Test: Biochemistry, Cell, and Molecular Biology
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The 5' cap on eukaryotic mRNA molecules is recognized by which of the following proteins?
The 5' cap on eukaryotic mRNA molecules is recognized by which of the following proteins?
The 5' cap is recognized by the important translation factor eIF4e. Once bound, eIF4e helps transport the mRNA molecule to the ribosome and facilitates bonding to the ribosomal machinery.
The 3' poly-A tail is recognized by PABP. RNA polymerase is involved in transcription, not translation. The 40s ribosomal subunit is recruited by the initiation complex (including eIF4e, PABP, and various other translation factors).
The 5' cap is recognized by the important translation factor eIF4e. Once bound, eIF4e helps transport the mRNA molecule to the ribosome and facilitates bonding to the ribosomal machinery.
The 3' poly-A tail is recognized by PABP. RNA polymerase is involved in transcription, not translation. The 40s ribosomal subunit is recruited by the initiation complex (including eIF4e, PABP, and various other translation factors).
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Chloramphenicol prevents protein translation by which of the following mechanisms?
Chloramphenicol prevents protein translation by which of the following mechanisms?
Tetracycline blocks the binding of aminoacyl tRNA to the A site of the ribosome.
Cyclohexamide blocks the translocation reaction on ribosomes.
Rifamycin blocks the initiation of RNA chains by binding to RNA polymerase.
Chloramphenicol blocks the pepidyl transferase reaction on the ribosome.
Tetracycline blocks the binding of aminoacyl tRNA to the A site of the ribosome.
Cyclohexamide blocks the translocation reaction on ribosomes.
Rifamycin blocks the initiation of RNA chains by binding to RNA polymerase.
Chloramphenicol blocks the pepidyl transferase reaction on the ribosome.
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During translation, which site in the ribosome allows for tRNA moelcules to enter the complex?
During translation, which site in the ribosome allows for tRNA moelcules to enter the complex?
The ribosomal complex has three sites where tRNA moelcules can be oriented during the process of translation: the A site, the P site, and the E site. During polypeptide elongation, a tRNA with an attached amino acid will enter at the A site. It will then move to the P site, now holding the growing polypeptide chain. All tRNAs no longer holding an amino acid will exit the ribosome at the E site.
The ribosomal complex has three sites where tRNA moelcules can be oriented during the process of translation: the A site, the P site, and the E site. During polypeptide elongation, a tRNA with an attached amino acid will enter at the A site. It will then move to the P site, now holding the growing polypeptide chain. All tRNAs no longer holding an amino acid will exit the ribosome at the E site.
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On which of the following molecules could you find an anticodon?
On which of the following molecules could you find an anticodon?
In order to make sure that the proper amino acid is added to the growing polypeptide chain, an anticodon found on the tRNA carrying the amino acid must be a match for the codon found on the mRNA.
In order to make sure that the proper amino acid is added to the growing polypeptide chain, an anticodon found on the tRNA carrying the amino acid must be a match for the codon found on the mRNA.
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Which of the following most accurately describes the chronological order of ribosome biogenesis in eukaryotes?
Which of the following most accurately describes the chronological order of ribosome biogenesis in eukaryotes?
Ribosomal proteins are translated in the cytoplasm and rRNA genes are transcribed in the nucleolus. Following protein translation, these proteins enter the nucleus through nuclear pores and localize to the nucleolus. Here, transcribed rRNA associates with the ribosomal proteins to form the 60S and 40S eukaryotic ribosomal subunits. Prokaryotes have 50S and 30S subunits. The ribosomal subunits then translocate to the cytoplasm where they join together to form fully functional ribosomes.
Ribosomal proteins are translated in the cytoplasm and rRNA genes are transcribed in the nucleolus. Following protein translation, these proteins enter the nucleus through nuclear pores and localize to the nucleolus. Here, transcribed rRNA associates with the ribosomal proteins to form the 60S and 40S eukaryotic ribosomal subunits. Prokaryotes have 50S and 30S subunits. The ribosomal subunits then translocate to the cytoplasm where they join together to form fully functional ribosomes.
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Which of the following is not an example of post-translational modification?
Which of the following is not an example of post-translational modification?
Polyadenylation is an example of post-transcriptional modification. This process involves adding large repeats of adenine bases to the 3' end of mRNA molecules, known as the poly-A tail.
Myristoylation is the process of adding myristate (a fatty acid) to a protein, alkylation is the process of adding an alkyl group, and ubiquination is the process of adding a molecule of ubiquitin (a small protein often used to signal degradation).
Polyadenylation is an example of post-transcriptional modification. This process involves adding large repeats of adenine bases to the 3' end of mRNA molecules, known as the poly-A tail.
Myristoylation is the process of adding myristate (a fatty acid) to a protein, alkylation is the process of adding an alkyl group, and ubiquination is the process of adding a molecule of ubiquitin (a small protein often used to signal degradation).
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In which of the following organelles does the initial linkage of a sugar for post-translation modification N-linked glycosylation most commonly occur?
In which of the following organelles does the initial linkage of a sugar for post-translation modification N-linked glycosylation most commonly occur?
Two of the more common types of glycosylation, N-linked and O-linked, occur at different points and in different places in the cell. N-linked glycosylation takes place in the lumen of the endoplasmic reticulum, while O-linked glycosylation takes place in the Golgi body.
The other options, the mitochondria and the nucleus, are not involved in these post-translational modifications.
Two of the more common types of glycosylation, N-linked and O-linked, occur at different points and in different places in the cell. N-linked glycosylation takes place in the lumen of the endoplasmic reticulum, while O-linked glycosylation takes place in the Golgi body.
The other options, the mitochondria and the nucleus, are not involved in these post-translational modifications.
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Please complete the following statement:
"The addition of a CH3CO group to the N-terminus of a protein is the most common form of protein modification. This chemical modification is called ________."
Please complete the following statement:
"The addition of a CH3CO group to the N-terminus of a protein is the most common form of protein modification. This chemical modification is called ________."
This question requires knowing either that CH3CO is an acetyl group, or that acetylation is the most common protein modification. Each of the other modifications described are biologically occurring modifications, but acetylation was the correct answer for the given statement.
This question requires knowing either that CH3CO is an acetyl group, or that acetylation is the most common protein modification. Each of the other modifications described are biologically occurring modifications, but acetylation was the correct answer for the given statement.
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In prokaryotes what site on the mRNA does the ribosome bind to initiate translation?
In prokaryotes what site on the mRNA does the ribosome bind to initiate translation?
The Shine-Dalgarno sequence is the ribosomal binding site in in prokaryotic mRNA that is located around 8 bases upstream of the start codon.
The Shine-Dalgarno sequence is the ribosomal binding site in in prokaryotic mRNA that is located around 8 bases upstream of the start codon.
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When conducting a stain of chromosomes, certain regions along the chromosome will stain more darkly than the rest. This is due to the fact that these regions are more tightly condensed. What is the functional outcome of having one region more condensed (heterochromatin) than the rest (euchromatin)?
When conducting a stain of chromosomes, certain regions along the chromosome will stain more darkly than the rest. This is due to the fact that these regions are more tightly condensed. What is the functional outcome of having one region more condensed (heterochromatin) than the rest (euchromatin)?
Heterochromatin often contains simple, repetitive sequences, and although it cannot be said that it is completely void of coding sequences, it is not typically transcribed. The tight wrapping prevents polymerase from accessing the strand, and euchromatin typically contains the regions that get transcribed. Thus, heterochromatin is though to contain repressed or inactive genes.
Heterochromatin often contains simple, repetitive sequences, and although it cannot be said that it is completely void of coding sequences, it is not typically transcribed. The tight wrapping prevents polymerase from accessing the strand, and euchromatin typically contains the regions that get transcribed. Thus, heterochromatin is though to contain repressed or inactive genes.
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Small GTPases are important molecular switches and signaling pathways. What proteins are responsible for promoting the activation of these small GTPases?
Small GTPases are important molecular switches and signaling pathways. What proteins are responsible for promoting the activation of these small GTPases?
The correct answer is guanine nucleotide exchange factors. In order to activate small GTPases and subsequently stimulate downstream pathways, guanine nucleotide exchange factors bind inactive GTPases and cause the release of guanine diphosphate (GDP). This allows guanine triphosphate (GTP) to bind and active the GTPase.
The correct answer is guanine nucleotide exchange factors. In order to activate small GTPases and subsequently stimulate downstream pathways, guanine nucleotide exchange factors bind inactive GTPases and cause the release of guanine diphosphate (GDP). This allows guanine triphosphate (GTP) to bind and active the GTPase.
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Which of the level of protein structure is incorrectly matched to its description?
Which of the level of protein structure is incorrectly matched to its description?
Primary structure of a protein is determined by covalent peptide bonds, and corresponds to the linear sequence of amino acids before structures begin to form. Secondary structure results from hydrogen bonding between the amino acid backbones to form alpha-helices and beta-sheets. Tertiary structure is formed when functional groups of the amino acids interact, either by hydrogen bonding, hydrophobic interactions, or disulfide bridge formation. Tertiary structure is associated with the three-dimensional structure of a single polypeptide chain. Quaternary structure forms when multiple polypeptide chains interact to build a multi-subunit structure.
Primary structure of a protein is determined by covalent peptide bonds, and corresponds to the linear sequence of amino acids before structures begin to form. Secondary structure results from hydrogen bonding between the amino acid backbones to form alpha-helices and beta-sheets. Tertiary structure is formed when functional groups of the amino acids interact, either by hydrogen bonding, hydrophobic interactions, or disulfide bridge formation. Tertiary structure is associated with the three-dimensional structure of a single polypeptide chain. Quaternary structure forms when multiple polypeptide chains interact to build a multi-subunit structure.
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Which of the following proteins are likely to contain leucine zipper domains?
Which of the following proteins are likely to contain leucine zipper domains?
Leucine zippers are domains that allow for the binding of DNA. The question is essentially asking, "which of these proteins are capable of binding DNA?"
Proteases cleave proteins, lipases hydrolyze lipids, and transmembrane proteins interact with membranes. Transcription factors are the only given proteins that bind DNA and, therefore, are much more likely to contain leucine zipper domains than the other options.
Leucine zippers are domains that allow for the binding of DNA. The question is essentially asking, "which of these proteins are capable of binding DNA?"
Proteases cleave proteins, lipases hydrolyze lipids, and transmembrane proteins interact with membranes. Transcription factors are the only given proteins that bind DNA and, therefore, are much more likely to contain leucine zipper domains than the other options.
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Which protein structure involves the binding of multiple polypeptides?
Which protein structure involves the binding of multiple polypeptides?
The structures of a protein increase in complexity all the way up to quaternary structure. Primary structure is based on the amino acid sequence of the protein, while secondary and tertiary structures are based on intermolecular attractions between the amino acids in the polypeptide. Quaternary structure is only seen when a functional protein complex is composed of two or more polypeptides bound together.
The structures of a protein increase in complexity all the way up to quaternary structure. Primary structure is based on the amino acid sequence of the protein, while secondary and tertiary structures are based on intermolecular attractions between the amino acids in the polypeptide. Quaternary structure is only seen when a functional protein complex is composed of two or more polypeptides bound together.
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Disulfide bonds in proteins are categorized under which structure class?
Disulfide bonds in proteins are categorized under which structure class?
The correct answer is more than one of these. Primary structure is defined as a succession of amino acids joined by peptide bonds. Secondary structure introduces dimensionality to a protein via hydrogen bonding to produce two predominant structures, alpha helices and beta-pleated sheets. Tertiary structures cause further protein folding by disulfide bonds between cysteines, Van der Waal interactions, and hydrophobic interactions. Quaternary structures involve multiple amino acid chains folding together, and utilize the same types of bonds as tertiary structures.
The correct answer is more than one of these. Primary structure is defined as a succession of amino acids joined by peptide bonds. Secondary structure introduces dimensionality to a protein via hydrogen bonding to produce two predominant structures, alpha helices and beta-pleated sheets. Tertiary structures cause further protein folding by disulfide bonds between cysteines, Van der Waal interactions, and hydrophobic interactions. Quaternary structures involve multiple amino acid chains folding together, and utilize the same types of bonds as tertiary structures.
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To which of the following structures in a typical molecule of tRNA is an amino acid attached?
To which of the following structures in a typical molecule of tRNA is an amino acid attached?
Amino acids are attached to the CCA tail of a tRNA. These are found at the 3' end of tRNA molecules and are important for recognition by aminoacyl tRNA synthetases (enzymes that actually attach the amino acids to the tRNA). The anticodon loop, as the name suggests, contains the anticodon, which will be important during translation for recognizing mRNA sequences. The D-loop and the variable loop are other portions of the tRNA that are important for maintaining structure and recognition.
Amino acids are attached to the CCA tail of a tRNA. These are found at the 3' end of tRNA molecules and are important for recognition by aminoacyl tRNA synthetases (enzymes that actually attach the amino acids to the tRNA). The anticodon loop, as the name suggests, contains the anticodon, which will be important during translation for recognizing mRNA sequences. The D-loop and the variable loop are other portions of the tRNA that are important for maintaining structure and recognition.
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How many ribosomal binding sites are there and what are their functions?
How many ribosomal binding sites are there and what are their functions?
The correct answer is there are three sites. A site binds aminoacyl-tRNA, P site binds peptidyl-tRNA, E site binds free tRNA before ribosomal exit.
The correct answer is there are three sites. A site binds aminoacyl-tRNA, P site binds peptidyl-tRNA, E site binds free tRNA before ribosomal exit.
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Which of the following is not a phase in translation?
Which of the following is not a phase in translation?
There are four phases in translation: activation, initiation, elongation, and termination. Activation is the process that joins the correct amino acid to the correct tRNA. When the tRNA has an amino acid bound to it, it is "charged." Initiation occurs when the small ribosomal subunit binds the 5' end of mRNA, with the help of initiation factors and other proteins. The structure then recruits a methionine tRNA to the start codon to begin the elongation process. Elongation occurs as charged tRNA molecules transfer their amino acids to the growing polypeptide. Termination results when a stop codon is recognized by release factors and the completed protein is released from the ribosome.
Modification of the transcript occurs after translation has been completed.
There are four phases in translation: activation, initiation, elongation, and termination. Activation is the process that joins the correct amino acid to the correct tRNA. When the tRNA has an amino acid bound to it, it is "charged." Initiation occurs when the small ribosomal subunit binds the 5' end of mRNA, with the help of initiation factors and other proteins. The structure then recruits a methionine tRNA to the start codon to begin the elongation process. Elongation occurs as charged tRNA molecules transfer their amino acids to the growing polypeptide. Termination results when a stop codon is recognized by release factors and the completed protein is released from the ribosome.
Modification of the transcript occurs after translation has been completed.
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Which of the following is not a type of modification that can occur after translation?
Which of the following is not a type of modification that can occur after translation?
Post-translational modifications that may occur after a protein is translated include numerous processes to alter the structure or function of the protein. Trimming modification involves removal of the N- or C - terminal propeptides from zymogens to generate mature proteins. Covalent alterations, including phosphorylation, glycosylation and hydroxylation, are frequently used to modify the structure or energy state of a protein. Proteasomal degradation requires the attachment of ubiquitin to defective proteins to tag them for degradation and digestion. Amino acids from degraded proteins can often be recycled to generate new molecules.
5' capping occurs in the nucleus after transcription and is required for transport of RNA out of the nucleus prior to translation.
Post-translational modifications that may occur after a protein is translated include numerous processes to alter the structure or function of the protein. Trimming modification involves removal of the N- or C - terminal propeptides from zymogens to generate mature proteins. Covalent alterations, including phosphorylation, glycosylation and hydroxylation, are frequently used to modify the structure or energy state of a protein. Proteasomal degradation requires the attachment of ubiquitin to defective proteins to tag them for degradation and digestion. Amino acids from degraded proteins can often be recycled to generate new molecules.
5' capping occurs in the nucleus after transcription and is required for transport of RNA out of the nucleus prior to translation.
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Which of the following ensures that viral gene translation occurs even when host translation is inhibited?
Which of the following ensures that viral gene translation occurs even when host translation is inhibited?
Viruses utilize IRES to allow translation to occur in a 5' cap-independent manner. Translational machinery (ribosomes) are located to the IRES so that translation can occur. 5' guanine cap and 3' poly-A tails are mRNA modifications that are normally necessary to initiate translation, but are cap-dependent. The promoter regulates genes expression on the level of transcription, whereas the 5' UTR regulates translation.
Viruses utilize IRES to allow translation to occur in a 5' cap-independent manner. Translational machinery (ribosomes) are located to the IRES so that translation can occur. 5' guanine cap and 3' poly-A tails are mRNA modifications that are normally necessary to initiate translation, but are cap-dependent. The promoter regulates genes expression on the level of transcription, whereas the 5' UTR regulates translation.
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