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Tamarin: Principles of Genetics, Seventh Edition
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III. Molecular Genetics
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11. Gene Expression: Translation
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The McGraw Hill Companies, 2001
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Gene Expression: Translation
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Ribosome
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Signal recognition particle Signal peptide (a) (d) GDP + Pi
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Membrane Translocon Docking protein (f)
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The signal hypothesis. A signal recognition particle recognizes a ribosome with a signal peptide, then draws the ribosome to a docking protein located near a translocon in the membrane. With the addition of GTP, the signal recognition particle releases the signal peptide; hydrolysis of the GTP to GDP Pi causes the signal recognition particle to leave the docking protein. Peptide synthesis then resumes, with the newly synthesized peptide passing through the translocon in the membrane. A signal peptidase on the other side of the membrane removes the signal peptide. When translation is completed, the ribosome dissociates and drops free of the translocon.
membrane.This speci city seems to depend on the exact signal sequence and membrane-bound glycoproteins called signal-sequence receptors. Apparently, after the ribosome binds to the docking protein, the signal peptide interacts with a signal-sequence receptor, which presumably determines whether that protein is specific for that membrane. If it is, the remaining processes continue. If not, the ribosome may be released from the membrane. The signal peptide does not seem to have a consensus sequence like the transcription or translation recognition boxes. Rather, similarities (at least for the endoplasmic reticulum and bacterial membrane-bound proteins) include a positively charged (basic) amino acid (commonly lysine or arginine) near the beginning
(N-terminal end), followed by about a dozen hydrophobic (nonpolar) amino acids, commonly alanine, isoleucine, leucine, phenylalanine, and valine (table 11.2).
Table 11.2 The Signal Peptide of the Bovine
Prolactin Protein*
NH2 - Met Asp Ser Lys Gly Ser Ser Gln Lys Gly Ser Arg Leu Leu Leu Leu Leu Val Val Ser Asn Leu Leu Leu Cys Gln Gly Val Val Ser | Thr Pro Val...Asn Asn Cys - COOH
Source: From Sasavage et al., Journal of Biological Chemistry, 257:678 81, 1982. Reprinted with permission. * The vertical line separates the signal peptide from the rest of the protein, which consists of 199 residues.
Tamarin: Principles of Genetics, Seventh Edition
III. Molecular Genetics
11. Gene Expression: Translation
The McGraw Hill Companies, 2001
Information Transfer
The Protein-Folding Problem
Since biochemist Christian An nsen won a 1972 Nobel Prize for showing that the enzyme ribonuclease refolds to its original shape after denaturation in vitro, scientists have believed that the nal protein shape (secondary and tertiary structure) forms spontaneously. Recently it has been shown, however, that many proteins do not normally form their nal active shape in vivo without the help of proteins called chaperones or molecular chaperones. The chaperones do not provide the threedimensional structure of the proteins they help, but rather bind to a protein in the early stages of folding to prevent unproductive folding or to allow denatured proteins to refold correctly. Like human chaperones, they prevent or undo incorrect interactions, according to J. Ellis. That is, many proteins have a large number of different structures they could fold into. Many of these structures would have no enzymatic activity or would form functionless aggregates with other proteins. Molecular chaperones allow proteins to fold into a thermodynamically stable and functional con guration. Each cycle of refolding requires ATP energy. A well-studied class of chaperones is known as the chaperonins, or Hsp60 proteins, because they are heat shock proteins about 60 kilodaltons (60,000 daltons) in size.They occur in bacteria, chloroplasts, and mitochondria. One of the best studied of these chaperonins is the protein GroE of E. coli. This protein in its active form is composed of two components, GroEL and GroES. GroEL (Hsp60) is made up of two disks, each composed of seven copies of a polypeptide. GroES (Hsp10) is a smaller component composed of seven copies of a small subunit. GroEL forms a barrel in which protein folding takes place ( g. 11.26).The barrel is shaped in such a way that entering proteins of a certain size make contact at interior points in either the upper or lower ring of GroEL (upper ring shown in g. 11.27). The attachment of GroES, the cap, causes the ring to open outward at the top, stretching the protein inside. This stretching takes energy from the hydrolysis of ATP molecules located inside the rings. When GroES dissociates, the protein can fold into a new, more functional, con guration. If it doesn t, the cycle repeats. There are several classes of molecular chaperones, proteins of different sizes and shapes that recognize different groups of proteins or protein conformations. GroEL recognizes about 300 different proteins, small enough to t into the barrel (20 60 kilodaltons) and having hydrophobic surfaces. These include many proteins in the transcription and translation machinery of the cell. Hsp90, another heat shock protein, recognizes proteins involved in signal transduction, discussed in chapter 16. Hsp70 recognizes hydrophobic regions in polypeptide side chains, many of which extend across membranes.
Electron micrograph of a chaperone protein (GroEL) from E. coli. Note the hollow, barrel shape of the protein. (Courtesy of Dr. R. W. Hendrix.)
The mitochondrion, which needs to import upwards of one thousand proteins through both inner and outer membranes, poses a speci c problem. Recent research has revealed a family of translocation proteins (called Tom proteins) in the outer membrane and a different set of translocation proteins (called Tim proteins) in the inner membrane.These proteins control the passage of proteins synthesized in the cytoplasm into the mitochondrion.
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