Ribossome Microscopic View



Interactions between tRNA and



Initiation of translation


Binding of tRNA to ribosome


Validation of mRNA-tRNA match

a protein that is essential for the movement of mRNA and ribosomes during eukaryotic protein synthesis.

Polysome formation increases the rate of protein synthesis

Several ribosomes can work simultaneously at translating a single mRNA molecule, producing multiple molecules of the protein at the same time. As soon as the first ribosome has moved far enough from the initiation point, a second initiation complex can form, then a third, and so on. An assemblage consisting of a thread of mRNA with its beadlike ribo-somes and their growing polypeptide chains is called a polyribosome, or polysome (Figure 12.13). Cells that are actively synthesizing proteins contain large numbers of polysomes and few free ribosomes or ribosomal subunits.

A polysome is like a cafeteria line, in which patrons follow one another, adding items to their trays. At any moment, the person at the start has a little food (a newly initiated protein); the person at the end has a complete meal (a completed protein). However, in the polysome cafeteria, everyone gets the same meal: Many copies of the same protein are made from a single mRNA.

While protein synthesis can be inhibited with antibiotics and speeded up via polysomes, these are not the only ways in which the amount of an active protein in a cell can be controlled. After the protein is synthesized, it may undergo changes that alter its function.

Posttranslational Events

A functional protein is not necessarily the same as the polypeptide chain that is released from the ribosome. Especially in eukaryotic cells, the polypeptide may need to be moved far from the site of synthesis in the cytoplasm, moved into an organelle, or even secreted from the cell. In addition, the polypeptide is often modified by the addition of new chemical groups that have functional significance. In this section, we examine these two posttranslational aspects of protein synthesis.

Chemical signals in proteins direct them to their cellular destinations

As a polypeptide chain emerges from the ribosome, it folds into its three-dimensional shape. As described in Chapter 3, this conformation is determined by the sequence of the amino acids that make up the protein, as well as by factors such as the polarity and charge of their R groups. Ultimately, the conformation of the polypeptide allows it to interact with other

Ribosomes Number Polysomes

Polypeptides grow longer as each ribosome moves toward the 3' end of mRNA.

12.13 A Polysome (a) A polysome consists of multiple ribosomes and their growing polypeptide chains moving in single file along an mRNA molecule. (b) An electron microscopic view of a polysome.

Polypeptides grow longer as each ribosome moves toward the 3' end of mRNA.

12.13 A Polysome (a) A polysome consists of multiple ribosomes and their growing polypeptide chains moving in single file along an mRNA molecule. (b) An electron microscopic view of a polysome.

molecules in the cell, such as a substrate or another polypeptide. In addition to this structural information, the amino acid sequence contains an "address label" indicating where in the cell the polypeptide belongs.

All protein synthesis begins on free ribosomes in the cytoplasm. As a polypeptide chain is made, the information contained in its amino acid sequence gives it one of two sets of instructions (Figure 12.14):

► "Finish translation and be released to the cytoplasm." Such proteins are sent to the nucleus, mitochondria, plastids, or peroxisomes, depending on the address in their instructions; or, lacking such specific instructions, they remain in the cytosol.

► "Stop translation, go to the endoplasmic reticulum (ER), and finish synthesis there." After protein synthesis is completed, such proteins may be retained in the ER or sent to lysosomes via the Golgi apparatus. Alternatively, they may be sent to the plasma membrane, or, lacking such specific instructions, they are secreted from the cell via vesicles that emanate from the plasma membrane.

destination: cytoplasm. After translation, some folded polypeptides have a short exposed sequence of amino acids that acts like a postal "zip code," directing them to an organelle. These signal sequences are either at the N ter-

12.14 Destinations for Newly Translated Polypeptides in a Eukaryotic Cell Signal sequences on newly synthesized polypeptides bind to specific receptor proteins on the outer membranes of the organelle to which they are "addressed." Once the protein has bound to it, the receptor forms a channel in the membrane, and the protein enters the organelle.

Prolys Inj

minus or in the interior of the amino acid chain. For example, the following sequence directs a protein to the nucleus:


This amino acid sequence occurs, for example, in the histone proteins associated with nuclear DNA, but not in citric acid cycle enzymes, which are addressed to the mitochondria.

The signal sequences have a conformation that allows them to bind to specific receptor proteins, appropriately called docking proteins, on the outer membrane of the appropriate organelle. Once the protein has bound to it, the receptor forms a channel in the membrane, allowing the protein to pass through to its organelle destination. (In this process, the protein is usually unfolded by a chaperonin so that it can pass through the channel, then refolds into its normal conformation.)

destination: endoplasmic reticulum. If a specific hydro-phobic sequence of about 25 amino acids occurs at the beginning of a polypeptide chain, the finished product is sent initially to the ER, and then to the lysosomes, the plasma membrane, or out of the cell. In the cytoplasm, before translation is finished, the signal sequence binds to a signal recognition particle composed of protein and RNA (Figure 12.15). This binding blocks further protein synthesis until the ribosome can become attached to a specific receptor protein in the membrane of the rough ER. Once again, the receptor protein is converted into a channel, through which the growing polypeptide passes. The elongating polypeptide may be retained in the ER membrane itself, or it may enter the interior space—the lumen—of the ER. In either case, an enzyme in the lumen of the ER

l| Protein synthesis begins on free ribosomes (ribosomes that are not attached to endoplasmic reticulum). The signal sequence is present on the polypeptide chain.

Interior of rough Signal endoplasmic reticulum recognition particle h h

Plasmé membrane mRNA


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