The Cytosol

Most Intermediary Metabolism Takes Place in the cytosol Degrades some small molecules ( ATP, proton gradient) Synthesizes ( for the structure, function, and growth cell) Cytosol generally represents about 55% of the total cell volume
Compartment Cytosol Mitochondria Rough ER cisternae Smooth ER cisternae + Golgi Nucleus Peroxisomes % cell vol 54 22 9 6 6 1 400 Number 1 1700 1 1

The Cytosol
Teeming with thousands of enzyme that catalyze the reaction: Glycolysis & gluconeogenesis ; biosintesa sugar, fatty acids, nucleotides and amino acids. Contains a variety of different cytoskeletal proteins

impart shape to cell, coherent cytoplasmic movement, and provide a general frame work that is used to help organize the many enzyme reaction

Many Proteins Are Synthesized by Ribosomes in the Cytosol

mRNA molecules emerge from the cell nucleus and become attached to large ribonucleoprotein particle called ribosomes. mRNA sequence is translated into a corresponding sequence of amino acid. Each ribosome is composed of a large and a small subunit Ribosomes are complex structures about 30 nm in the large rRNA molecule form a framework on which

KROMOSOM DAN DNA

The Binding of Many Ribosomes to an Individual Messenger RNA Molecule Generates Polysomes The initiation codon AUG, which is recognized by a special initiator tRNA (incorporating methionine) that must pair with the AUG codon in order to initiate each new polypeptide chain. Driven by the energy of GTP hydrolysis, the ribosome then moves along the mRNA in the 5 to 3 direction to begin the elongation stage. At each step of elongation, the specific aminoacyl tRNA molecule whose anticodon is complementary to the next codon in the mRNA binds to the ribosome.

Protein Synthesis Is Blocked by Specific Inhibitors There are many drugs and toxins that specifically affect each of the major steps of protein synthesis, and these have been very useful for working out cellular menchanisms, Chloramphenicol, Cycloheximide, puromycin The first two drugs reversibly inhibit peptidyl transferase, the ribosomal enzyme that forms peptide bonds. Chloramphenicol inhibit protein synthesis only on the ribosomes in the mitochondria/chloroplast, cycloheximide affects only cytosolic ribosome Puromycin is a structural analogue of a tRNA molecule linked to an

Some Protein Regulate the Rate of Their Own Synthesis by Binding to the Messenger RNA Molecules on Which They Are Made The intracellular concentration of a protein must be closely regulated because an excess would harm the cell. Examples: ribosomal protein, many of which will bind to RNA molecule indiscriminately if more are present than can be bound by the available rRNA. When multiple copies of one of the ribosomal protein genes are inserted into E. coli, the amout of messenger RNA coding for that protein increase dramatically, but the rate of synthesis of the protein itself increase only slightly.

In Eucayotes Only One Species of Polypeptide Chain Can Be Synthesized on Each Messenger RNA Molecule Eucaryotic and procaryotic messenger RNAs ;differ some what in both structure dan function. Eucaryotic mRNAs are modified in the nucleus immediately after their transcription. As a result, they usually carry both a unique cap structure, composed of a 7-methylguanosine residu lingked to a triphosphate, at their 5 end and a run of about 200 adenylic residues (poly A) at their 3 end. Procaryotic mRNAs are quite different from eucaryoutic mRNAs. Bacterial mRNAs have no 3 poly A or 5 cap structure. Bacterial messenger RNAs are commonly polycistronic,

Polyprotein Are Often Made in Eucaryotes Related enzymatic activities can be encoded by the same messenger RNA molecule in eucaryotes. mRNA is translated into a single, large multifunctional protein. Polyprotein is cleaved by specific proteases to yield distinct enzymes. In other cases, however, it remains intact as a single multifunctional polypeptide. A series of related enzymatic activities can be linked together in a polyprotein in eucaryotes, while in procaryotes the same enzymatic activities often involve the noncovalent complexing of separate enzyme

Many Proteins Undergo Covalent Modification After Their Synthesis Protein undergo some type of covalent modification after being released from the ribosome. More than 100 different such modifications of the amino acid side chain are known. Example: phosphorylation of a selected free OH group of the amino acid side chain of a serine, a threonine, or a tyrosine residue in a protein. Enzyme called protein kinases utilize ATP to phosphorylate proteins in this way. Protein phosphorylation is reversible because of the abundant phosphatase present in the cytosol.

Many Proteins Undergo Covalent Modification After Their Synthesis There are numerous other irreversible modifications whose exact function are less clear. Exp: the amino terminus of many proteins in the cyto sol is modified (blocked) by acetylation, and the amino group on a few selected lysines can be metylated. Many other permanent permanent covalent modifications occur only to those proteins that leave the cytosol for other intracellular destinations. Exp.:

In the ER, almost half of the proline residues in the secrete protein collagen are hyddroxylated to hydroxyproline. Addition of a second carboxyl group to glutamic acid residues in proteins to form -carboxyglutamete, a dicarxylic acid with a high affinity for 2++ Ca

Some Proteins Are Degraded Soon After They Have Been Synthesized Concentration of protein in a cell is determined by the balance between the rate of its synthesis and the rate of its degradation. As a result, there is a constant Protein turnover. The rate of synthesis of a protein is usually controlled by regulating the amount of its mRNA available for translation. In addition, a cell can contorol the concentration of a protein by regula ting the rate at which the protein is destroyed. Most proteins are compact structures, inherntly somewhat resistant to roteolytic attack and, therefore, to degradation. Many of the normal proteins that are subject to rapid

Not All Proteins Synthesized in the Cytosol Remain There Many of the proteins destined for a variety of intracellular organelles and their membranes, as well as all known proteins destined for secretion are synthesized by such ribosomes. But some of the proteins translated by free ribosomes in the cytosol also leave the cytosol. Example :

Histones, as well as many other chromatin proteins, rapidly diffuse through large nuclear pores and bind to structures in the nucleus followinng their synthesis in the cytoplasm.

Most of the proteins in chloroplasts and mitochondria,

The Cytosol
The cytosol sonsists of all of the space outside the cellular organelles and generally represents 50%-60% of the total cell vol. Most intermediary metabolism and the protein synthesis required for cell growth and maintenance occur in the cytosol. The amount of any jparticular protein in a cell depends on the balance between the rate at which its mRNA is synthesizedin the nucleus and the rate rate at which it is degraded. Some protein are degraded rapidly and continuously in cells, presumably to allow rapid changes in their concentrations in response to regulatory signals.