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By the end of this section, you will be able to:
  • Understand the process of translation and discuss its key factors
  • Describe how the initiation complex controls translation
  • Explain the different ways in which the post-translational control of gene expression takes place

After the RNA has been transported to the cytoplasm, it is translated into protein. Control of this process is largely dependent on the RNA molecule. As previously discussed, the stability of the RNA will have a large impact on its translation into a protein. As the stability changes, the amount of time that it is available for translation also changes.

The initiation complex and translation rate

Like transcription, translation is controlled by proteins that bind and initiate the process. In translation, the complex that assembles to start the process is referred to as the initiation complex    . The first protein to bind to the RNA to initiate translation is the eukaryotic initiation factor-2 (eIF-2)    . The eIF-2 protein is active when it binds to the high-energy molecule guanosine triphosphate (GTP) . GTP provides the energy to start the reaction by giving up a phosphate and becoming guanosine diphosphate (GDP) . The eIF-2 protein bound to GTP binds to the small 40S ribosomal subunit . When bound, the methionine initiator tRNA associates with the eIF-2/40S ribosome complex, bringing along with it the mRNA to be translated. At this point, when the initiator complex is assembled, the GTP is converted into GDP and energy is released. The phosphate and the eIF-2 protein are released from the complex and the large 60S ribosomal subunit binds to translate the RNA. The binding of eIF-2 to the RNA is controlled by phosphorylation. If eIF-2 is phosphorylated, it undergoes a conformational change and cannot bind to GTP. Therefore, the initiation complex cannot form properly and translation is impeded ( [link] ). When eIF-2 remains unphosphorylated, it binds the RNA and actively translates the protein.

Art connection

The eIF2 protein is a translation factor that binds to the small 40S ribosome subunit. When eIF2 is phosphorylated, translation is blocked.
Gene expression can be controlled by factors that bind the translation initiation complex.

An increase in phosphorylation levels of eIF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s. What impact do you think this might have on protein synthesis?

Chemical modifications, protein activity, and longevity

Proteins can be chemically modified with the addition of groups including methyl, phosphate, acetyl, and ubiquitin groups. The addition or removal of these groups from proteins regulates their activity or the length of time they exist in the cell. Sometimes these modifications can regulate where a protein is found in the cell—for example, in the nucleus, the cytoplasm, or attached to the plasma membrane.

Chemical modifications occur in response to external stimuli such as stress, the lack of nutrients, heat, or ultraviolet light exposure. These changes can alter epigenetic accessibility, transcription, mRNA stability, or translation—all resulting in changes in expression of various genes. This is an efficient way for the cell to rapidly change the levels of specific proteins in response to the environment. Because proteins are involved in every stage of gene regulation, the phosphorylation of a protein (depending on the protein that is modified) can alter accessibility to the chromosome, can alter translation (by altering transcription factor binding or function), can change nuclear shuttling (by influencing modifications to the nuclear pore complex), can alter RNA stability (by binding or not binding to the RNA to regulate its stability), can modify translation (increase or decrease), or can change post-translational modifications (add or remove phosphates or other chemical modifications).

The addition of an ubiquitin group to a protein marks that protein for degradation. Ubiquitin acts like a flag indicating that the protein lifespan is complete. These proteins are moved to the proteasome    , an organelle that functions to remove proteins, to be degraded ( [link] ). One way to control gene expression, therefore, is to alter the longevity of the protein.

Multiple ubiquitin groups bind to a protein. The tagged protein is then fed into the hollow tube of a proteasome. The proteasome degrades the protein.
Proteins with ubiquitin tags are marked for degradation within the proteasome.

Section summary

Changing the status of the RNA or the protein itself can affect the amount of protein, the function of the protein, or how long it is found in the cell. To translate the protein, a protein initiator complex must assemble on the RNA. Modifications (such as phosphorylation) of proteins in this complex can prevent proper translation from occurring. Once a protein has been synthesized, it can be modified (phosphorylated, acetylated, methylated, or ubiquitinated). These post-translational modifications can greatly impact the stability, degradation, or function of the protein.

Art connections

[link] An increase in phosphorylation levels of eIF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s. What impact do you think this might have on protein synthesis?

[link] Protein synthesis would be inhibited.

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Questions & Answers

What is Staining?
Fazal Reply
what is biology
Biology is the study of life
what is biology
Ysabella Reply
biology is a study of living things
Biology is a diverse branch of science that deals with mostly living things
What happen when inhibit the transcription?
what is the effect of not doing sexual intercourse
what is the mechanism of cellular respiration
Rita Reply
what is enzyme
garry Reply
They are organic catalysts that alter the rate of chemical reactions in the body.
meaning they speed up reaction
Enzymes are forms of chemicals that are specialized in their own areas.(eg digestion of food)
Enzymes are organic catalysts
what is a cell
Praize Reply
Basic Functional Unit of Life
what is biology
Mordi Reply
biology is the study of living organisms and their interactions with one another and their environments
which of the following event does not occur during some stages of interface?
Bangha Reply
What is microfilaments
KHalid Reply
What is multicellular organisms
Ovie Reply
these are organisms with more than two cells
the process when a male toad fertilizer a female eggs is called what?
Ahrebe Reply
how did unicellular organisms form plants and animals or is it that different unicellular organisms formed plants and animald
YXNG Reply
name the components of faeces
undigested carbohydrate, fibre
what are unicellular organisms..?
they have only one cell
faeces contains many undigested food materials, after the food has been digested then it will be absorbed in the blood stream for assimilation.,......... but the remains toxic materials are stored in the rectum these toxic materials are the faeces and it contains bile salts, the polysaccharides .
unicellular organisms are the ones with only single cell.
thanks for your answers guys.
what is class bryophyta
Emefa Reply
how many stages do we have in glycolysis?
10 stages
the presence of a membrane enclosed nuclosed is a characteristics of what
Addai Reply
eukaryotic cell

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Source:  OpenStax, Biology. OpenStax CNX. Feb 29, 2016 Download for free at http://cnx.org/content/col11448/1.10
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