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What is the role of messenger RNA and ribosomes in protein synthesis

It is still not fully known , exactly when and how, the actual modification of a given amino acid residue occurs, at which stage of synthesis, within a protein molecule .

In eukaryotic cells, ATP is synthesizedprimarily on the inner membrane of the mitochondria.

It is an extension of the outer membrane of the nuclear envelope, so allowing mRNA to be transported swiftly to the 80s ribosomes, where they are translated in protein synthesis

Ribosomes are the structures in which protein synthesis takes place

Continuous elongation requires longer term metabolic changes such as protein synthesis.

are the monomers which are to produce proteins. Amino acid synthesis is the set of processes () which build the amino acids from carbon sources like .

The synthesis of proteins is known as translation. Translation occurs in the where the are located. Ribosomes are made of a small and large subunit which surrounds the mRNA. In translation, is decoded to produce a specific according to the rules specified by the trinucleotide . This uses an mRNA sequence as a template to guide the synthesis of a chain of that form a protein. Translation proceeds in four phases: activation, initiation, elongation and termination (all describing the growth of the amino acid chain, or that is the product of translation).

which are in the process of synthesizing proteins for secretion or ..

The 4 compounds elicited similar inhibitory effects on the synthesis of protein, RNA, and DNA.

In general , protein molecules are believed to be modified by small chemical groups, post-translationally. Chemical modifications such as, phosphorylation of serine / threonine, acetylation or methylation of lysine, hydroxylation of proline / lysine, formylation of glycine , glycosylation of serine / threonine / asparagine, acylation of cysteine , myristoylation of glycine , biotinylation of lysine, ubiquitination , etc. on proteins is a very important issue in relation to properly understand the biological functions of a given protein. These post- translational modifications are studied hard and well-established with the discovery of the respective enzymes (kinases for phosphorylation, acetylases for acetylation, methyl transferases for methylation, etc. ) which carry on the chemical modifications on the specific amino acid residues . All of these modifications are still believed to be happened as post-translational events ; There is no study yet on when actually one particular modification occurs on a given amino acid residue in a given protein . Does it happen when the protein is already formed, or, when the amino acid chain is being synthesized, or before the translation of the primary chain has begun?

In activation, the correct amino acid (AA) is joined to the correct . While this is not technically a step in translation, it is required for translation to proceed. The AA is joined by its carboxyl group to the 3' OH of the tRNA by an ester bond. When the tRNA has an amino acid linked to it, it is termed "charged". Initiation involves the small subunit of the ribosome binding to 5' end of mRNA with the help of (IF), other proteins that assist the process. Elongation occurs when the next aminoacyl-tRNA (charged tRNA) in line binds to the ribosome along with and an . Termination of the polypeptide happens when the A site of the ribosome faces a stop codon (UAA, UAG, or UGA). When this happens, no tRNA can recognize it, but can recognize nonsense codons and causes the release of the polypeptide chain. The capacity of disabling or inhibiting translation in protein biosynthesis is used by such as: , , , , , , etc.

Proteins that are destined to remain in the cytosol complete their synthesis on free ribosomes and are therefore released into the cytosol.
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the ER to the plasma membrane when protein secretion is ..

The DNA is transcribed into a variety of RNA intermediates. The last version is used as a template in synthesis of a chain. Proteins can often be synthesized directly from genes by . When a protein is harmful and needs to be available on short notice or in large quantities, a is produced. A is an inactive protein containing one or more that can be activated when the inhibitory sequence is removed by during . A is a form that contains a signal sequence (an N-terminal ) that specifies its insertion into or through membranes; i.e., targets them for secretion. The signal peptide is cleaved off in the . have both sequences (inhibitory and signal) still present.

Protein synthesis - The Full Wiki

Protein synthesis is the process in which build . The term is sometimes used to refer only to protein but more often it refers to a multi-step process, beginning with and of into which is then used as input to translation.

Protein synthesis is the process in which cells build proteins

For synthesis of protein, a succession of molecules charged with appropriate amino acids have to be brought together with an mRNA molecule and matched up by base-pairing through their anti-codons with each of its successive codons. The amino acids then have to be linked together to extend the growing protein chain, and the tRNAs, relieved of their burdens, have to be released. This whole complex of processes is carried out by a giant multimolecular machine, the , formed of two main chains of RNA, called ribosomal RNA (), and more than 50 different proteins. This molecular juggernaut latches onto the end of an mRNA molecule and then trundles along it, capturing loaded tRNA molecules and stitching together the amino acids they carry to form a new protein chain.

modification in a cell-free protein synthesis system having a ..

Disulfide bridges are found only in proteins that are to be secreted or are exterior membrane proteins, since the cytosol contains reducing agents that would break these S-S bonds.

Protein synthesis Cells are capable of ..

Since these chemical modifications are related to the biological functions of a protein, it is easy to think that these chemical modifications are happened to the whole protein molecule , after the protein primary chain is fully synthesized ; but , if that is the case, we have to consider the fact that the primary chains get folded instantly, (in a similar way as the newly synthesized DNA strands form helixes), to attain its compact-globular conformation ; As most of the primary chains are fairly long [a 5Kd protein may have 40-45 amino acid residues in its primary chain], it is likely that the newly formed amino acid chain tries to remain intact by folding thereby avoiding its breakdown via lots of proteases present within the cytoplasm. And, no capping event to protect the N-terminal end of the primary sequence (similar to 5' m-RNA capping to protect m-RNAs) is ever discovered for protein primary structure .So, by folding mechanism the primary chain perhaps avoids the protease attacks . However, once it gets folded, it may be very difficult for the respective enzyme molecule to find out the particular aa residue from the complexity of that compactly folded conformation . In addition, it can be clearly imagined that this enzymatic modification/reaction on a given amino acid requires presence and association of the appropriate enzyme, necessary cofactors, etc ; This association is much easier to occur when the amino acid residues in the primary structure are readily available for binding ; in other words , it is much difficult for the enzyme molecules to find and to bind to its substrate amino acid residue in a mature protein molecule after its three-dimentional conformation been attained .

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