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What would happen if a eukaryotic ribosome had only one tRNA binding site instead of the P and A sites we see in today eukaryotic ribosomes and still needed to execute translation?
Wiki User
∙ 12y ago
no translation occur bcoz the polypeptide chain formed at p site , a for attachment, p for polypeptide bond formation, e for exit site. so .......................................?
Wiki User
∙ 12y ago
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What does Chloramphenicol do?
Chloramphenicol is a broad spectrum antibiotic. It functions by inhibiting protein synthesis in bacterial cells by binding to the ribosome. The ribosomes of prokaryotic cells are 70S where as eukaryotes have 80S ribosomes, this fundimental difference means that chloamphenicol specifcally targets bacterial protein synthesis. It is effective against Gram positive as well as Gram negative bacteria.
What will happen after the ribosome joins the methionine and phenylalanine?
The ribosome breaks he bond between methionine and it's tRNA. The tRNA floats away from the ribosome, allowing the ribosome to bend to another tRNA. The ribosome moves along the mRNA, binding new tRNA molecules and amino acids.
What are the names of the three RNA strands?
Ribosomes are the components of cells that make proteins from amino acids. One of the central tenets of biology is that DNA makes RNA, which then makes protein. The DNA sequence in genes is copied into a messenger RNA (mRNA). Ribosomes then read the information in this RNA and use it to produce proteins. Ribosomes do this by binding to a messenger RNA and using it as a template for the correct sequence of amino acids in a particular protein. The amino acids are attached to transfer RNA (tRNA) molecules, which enter one part of the ribosome and bind to the messenger RNA sequence. The attached amino acids are then joined together by another part of the ribosome. The ribosome moves along the mRNA, "reading" its sequence and producing a chain of amino acids.Ribosomes are made from complexes of RNA and protein. Ribosomes are divided into two subunits, one larger than the other. The smaller subunit binds to the mRNA, while the larger subunit binds to the tRNA and the amino acids. When a ribosome finishes reading a mRNA these two subunits split apart. Ribosomes have been classified as ribozymes, since the ribosomal RNA seems to be most important for the peptidyl transferase activity that links together amino acids.Ribosomes from bacteria, archaea and eukaryotes (the three domains of life on Earth), have significantly different structure and RNA sequences. These differences in structure allow some antibiotics to kill bacteria by inhibiting their ribosomes, while leaving human ribosomes unaffected. The ribosomes in the mitochondria of eukaryotic cells resemble those in bacteria, reflecting the evolutionary origin of this organelle.[1] The word ribosome comes from ribonucleic acid and the Greek: soma (meaning body).
Which cell organelle puts amino acids together in a specific order to make proteins?
This would be the function of the ribosomes. The ribosome assembles amino acids into proteins. Ribosomes are small structures made of ribosomal RNA (rRNA) and protein. (RNA is a molecule similar in structure to DNA.) When cells need to make proteins, they copy the instructions for the protein from the DNA of the cell by making a molecule of messenger RNA (mRNA). The mRNA travels to the ribosomes in the cytoplasm of the cell. Another type of RNA molecule, called transfer RNA (tRNA) brings amino acids to the ribosome. The tRNA molecules decode the mRNA by binding to it, so that the tRNAs bring in the correct amino acids according to the instructions in the mRNA. The ribosome helps keep this whole process organized and helps form the bonds between the amino acids to create a chain of amino acids. A chain of amino acids is called a polypeptide chain. Polypeptide chains fold up to form proteins.
What is role of maskin protein?
Maskin protein prevents eukaryotic mRNAs from being recruited to the ribosome prior to egg fertilization. In other words, maskin halts translation of certain mRNA until after fertilization. In the 3' end of the mRNA there is an Untranslated Region (UTR) (often a rich A region) that does not code for amino acids of the protein. Instead regions of the UTR are binding sites for Cytoplasmic Poly A Element-Binding Protein (CPEB), which binds to maskin. (Other translation inhibitors have similar mechanisms.) This interaction acts to prevent assembly of translation of the mRNA initiation complex until after fertilization. Upon fertilization, phosphorylation of CPEB causes it to undergo a conformational alteration and release from the UTR. Translation can then proceed. Poly(A) binding protein (PBAP) is able to bind to the now open A-rich UTR. PBAP binds to the initiation factor eIF-4G, which is bound to eIF-4E, another initiation factor bound to the 5' cap on the 5' end of mRNA. This binding forms the characteristic loop structure of eukaryotic protein synthesis. Sources: Karp, Gerald C. Cell and Molecular Biology: Concepts and Experiments. edition 5 See the related link for further information.
How many binding sites are found on the ribosomes?
The ribosome has three sites for binding. It binds RNA and DNA so that they can be matched to their complementary base pair.
Observe how the mRNA interacts with the ribosome in the simulation. How is this interaction similar to what actually happens in translation?
The interaction between mRNA and ribosomes in the simulation is meant to reflect the process of translation that occurs in cells. During translation, the ribosome uses the information stored in the mRNA molecule to synthesize a protein. The ribosome moves along the mRNA molecule and reads its codons (sets of three nucleotides) to determine which amino acids should be added to the growing polypeptide chain. In the simulation, the mRNA molecule is represented as a linear sequence of codons, and the ribosome is represented as a moving object that recognizes and interacts with the codons. The ribosome moves along the mRNA and recognizes each codon by binding to it. This interaction is similar to what happens in real cells, where the ribosome recognizes codons by binding to specific sites on the mRNA molecule. In the simulation, the ribosome can also interact with tRNA molecules, which bring the correct amino acids to the ribosome for incorporation into the growing polypeptide chain. This is similar to what happens in real cells, where tRNA molecules bring the correct amino acids to the ribosome for use in protein synthesis. Overall, the interaction between mRNA and ribosomes in the simulation is meant to closely resemble the process of translation that occurs in cells.
How does tetracycline affect a bacterial cell?
The antibiotic binds to the ribosome of the prokaryotic cell, so it inhibits the proteins translation, hence the cell dies. You have to consider that prokariotic ribosome it´s different to eukaryotic ribosome, so this antibiotic doesn´t affect our cells, only the target bacteria
What happens at the end of translation in the p site?
the amino acids detach from the ribosome
What is the subunit of a ribosome has binding sites for trna?
A site
Observe how the mRNA interacts with the ribosome in the simulation. How is this interaction different than what actually happens in translation?
Urur7
What do ribosomes do in order to make proteins?
Ribosomes are the components of cells that make proteins from all amino acids. One of the central tenets of biology, often referred to as the "central dogma," is that DNA is used to make RNA, which, in turn, is used to make protein. The DNA sequence in genes is copied into a messenger RNA (mRNA). Ribosomes then read the information in this RNA and use it to create proteins. This process is known as translation; i.e., the ribosome "translates" the genetic information from RNA into proteins. Ribosomes do this by binding to an mRNA and using it as a template for the correct sequence of amino acids in a particular protein. The amino acids are attached to transfer RNA (tRNA) molecules, which enter one part of the ribosome and bind to the messenger RNA sequence. The attached amino acids are then joined together by another part of the ribosome. The ribosome moves along the mRNA, "reading" its sequence and producing a chain of amino acids
How are ribosomes recycled?
After translation stops and the polypeptide chain has been released, the ribosome needs to dissociate off of the mRNA transcript. A Ribosome Recycling Factor (RRF) will insert itself into the A-pocket of the ribosome (this A-pocket still contains a stop codon). Elongation Factor G (EF-G) then binds to the RRF. This binding stimulates the release of the two tRNAs that are in the P and E pockets of the ribosome. The RRF and the EF-G are then displaced from the ribosome. The mRNA is also released and the two halves of the ribosome are allowed to dissociate. Afterwards, the small ribosomal subunit is either bound by IF1 an IF3 or elF1 and eLF1A depending on the organism being a prokaryote or eukaryote. These proteins block tRNAs from entering into its E and A pockets.
One binding site on a ribosome holds an mRNA molecule and the other two binding?
tRNA molecules.
What is the role of mRNA after it leaves the nucleus and enters the cytoplasm of a eukaryotic cell?
Transcription takes place in the nucleus. This process produces mature mRNA once the noncoding introns were removed. This mRNA then enters the cytoplasm to be translated. Translation occurs on the ribosome and it involves tRNA binding to the codon(on the mRNA). This process is known as protein synthesis
What are the two bonding sites of tRNA on the ribosomes?
tRNA has two binding sites on the ribosome first one is A-site (aninoacyl -tRNA binding site), and second one is P-site (peptidyl-tRNA binding site) and E-site (Exit site)
What does Chloramphenicol do?
Chloramphenicol is a broad spectrum antibiotic. It functions by inhibiting protein synthesis in bacterial cells by binding to the ribosome. The ribosomes of prokaryotic cells are 70S where as eukaryotes have 80S ribosomes, this fundimental difference means that chloamphenicol specifcally targets bacterial protein synthesis. It is effective against Gram positive as well as Gram negative bacteria.
