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Berg JM, Tymoczko JL, Stryer L. Biochemistry. 5th edition. New York: W H Freeman; 2002.

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Biochemistry. 5th edition.

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Section 12.7Eukaryotic Cells Contain Compartments Bounded by Internal Membranes

Thus far we have considered only the plasma membrane of cells. Many bacteria such as E. coli have two membranes separated by a cell wall (made of proteins, peptides, and carbohydrates) lying in between (Figure 12.35). The inner membrane acts as the permeability barrier, and the outer membrane and the cell wall provide additional protection. The outer membrane is quite permeable to small molecules owing to the presence of porins. The region between the two membranes containing the cell wall is called the periplasm. Other bacteria and archaea have only a single membrane surrounded by a cell wall.

Figure 12.35. Cell Membranes of Prokaryotes.

Figure 12.35

Cell Membranes of Prokaryotes. A schematic view of the membrane in bacterial cells surrounded by (A) two membranes or (B) one membrane.

Eukaryotic cells, with the exception of plant cells, do not have cell walls, and their cell membranes consist of a single lipid bilayer. In plant cells, the cell wall is on the outside of the plasma membrane. Eukaryotic cells are distinguished by the use of membranes inside the cell to form internal compartments (Figure 12.36). For example, peroxisomes, organelles that play a major role in the oxidation of fatty acids for energy conversion, are defined by a single membrane. Mitochondria, the organelles in which ATP is synthesized, are surrounded by two membranes. Much like the case for a bacterium, the outer membrane is quite permeable to small molecules, whereas the inner membrane is not. Indeed, considerable evidence now indicates that mitochondria evolved from bacteria by endosymbiosis (Section 18.1.2). A double membrane also surrounds the nucleus. However, the nuclear envelope is not continuous but, instead, consists of a set of closed membranes that come together at structures called nuclear pores. These pores regulate transport into and out of the nucleus. The nuclear membranes are linked to another membrane-defined structure, the endoplasmic reticulum, which plays a host of cellular roles, including drug detoxification and the modification of proteins for secretion (Section 11.3.4). Thus, a eukaryotic cell comprises interacting compartments, and transport into and out of these compartments is essential to many biochemical processes.

Figure 12.36. Internal Membranes of Eukaryotes.

Figure 12.36

Internal Membranes of Eukaryotes. Electron micrograph of a thin section of a hormone-secreting cell for the rat pituitary, showing the presence of internal structures bounded by membranes. [Biophoto Associates/Photo Researchers.]

12.7.1. Proteins Are Targeted to Specific Compartments by Signal Sequences

The compartmentalization of eukaryotic cells makes possible many processes that must be separated from the remainder of the cellular environment to function properly. Specific proteins are found in peroxisomes, others in mitochondria, and still others in the nucleus. How do proteins end up in the proper compartment? Even for bacteria, some targeting of proteins is required: some proteins are secreted from the cell, whereas others remain in the cytosol.

Proteins include specific sequences that serve as address labels to direct the molecules to the proper location. For example, most peroxisomal proteins end with a sequence, Ser-Lys-Leu-COO- , that acts as an autonomous targeting signal. The removal of this sequence from a protein that normally resides in peroxisomes blocks its import into that organelle, whereas the addition of this sequence to a protein that normally resides in the cytosol can direct that protein to peroxisomes. A protein destined to pass through both mitochondrial membranes usually has a targeting sequence at its amino terminus (Figure 12.37). Unlike the peroxisomal targeting sequence, these amino-terminal sequences are highly variable; no clear consensus exists. They are typically from 15 to 35 residues long and rich in positively charged residues and in serines and threonines. Proteins destined for the nucleus have internal targeting sequences. A typical nuclear localization signal contains five consecutive positively charged residues such as Lys-Lys-Lys-Arg-Lys. The addition of such a sequence to a protein not found in the nucleus can direct it to the nucleus (Figure 12.38). Other sequences can direct proteins out of the nucleus. The known targeting sequences are given in Table 12.4.

Figure 12.37. A Mitochondrial Targeting Sequence.

Figure 12.37

A Mitochondrial Targeting Sequence. This sequence is recognized by receptors on the external face of the outer mitochondrial membrane. A protein bearing the sequence will be imported into the mitochondrion. Hydrophobic residues are shown in yellow, basic (more...)

Figure 12.38. Movement of a Protein Into the Nucleus.

Figure 12.38

Movement of a Protein Into the Nucleus. Localization of (A) unmodified pyruvate kinase, and (B) pyruvate kinase containing a nuclear localization signal sequence attached to its amino terminus. The protein was visualized by fluorescence microscopy after (more...)

Table 12.4. Targeting sequences.

Table 12.4

Targeting sequences.

Targeting sequences act by binding to specific proteins associated with each organelle. The determination of the structure of a protein, α-karyopherin, that binds to the nuclear localization signal reveals how the protein recognizes such a targeting sequence (Figure 12.39). A peptide containing the appropriate sequence binds to a specific site on the protein. The target peptide is held in an extended conformation through interactions between the target peptide backbone and asparagine side chains of the α-karyopherin while each of the basic residues lies in a deep pocket near the bottom, lined with negatively charged residues. Proteins that bind to the other targeting signal sequences presumably also have structures that allow recognition of the required features. Note that we have considered only how proteins are marked for different compartments. Later, we will consider the mechanisms by which proteins actually cross membranes (Section 11.3.2).

Figure 12.39. Protein Targeting Signal Recognition.

Figure 12.39

Protein Targeting Signal Recognition. Image mouse.jpg The structure of the nuclear localization signal-binding protein α-karyopherin (also known as α-importin) with a nuclear localization signal peptide bound to its major recognition site.

12.7.2. Membrane Budding and Fusion Underlie Several Important Biological Processes

Membranes must be able to separate or join together to take up, transport, and release molecules. Many take up molecules through the process of receptor- mediated endocytosis (Figure 12.40). Here, a protein or larger complex initially binds to a receptor on the cell surface. After the protein is bound, specialized proteins act to cause the membrane in the vicinity of the bound protein to invaginate. The invaginated membrane eventually breaks off and fuses to form a vesicle.

Figure 12.40. Receptor-Mediated Endocytosis.

Figure 12.40

Receptor-Mediated Endocytosis. The process of receptor-mediated endocytosis is illustrated for the cholesterol-carrying complex, low-density lipoprotein (LDL): (1) LDL binds to a specific receptor, the LDL receptor; (2) this complex invaginates to form (more...)

Receptor-mediated endocytosis plays a key role in cholesterol metabolism (Section 26.3.3). Some cholesterol in the blood is in the form of a lipid-protein complex called low-density lipoprotein (LDL). Low density lipoprotein binds to an LDL receptor, an integral membrane protein. The segment of the plasma membrane containing the LDL-LDL receptor complex then invaginates and buds off from the membrane. The LDL separates from the receptor, which is recycled back to the membrane in a separate vesicle. The vesicle containing the LDL fuses with a lysosome, an organelle containing an array of digestive enzymes. The cholesterol is released into the cell for storage or use in membrane biosynthesis, and the remaining protein components are degraded. Various hormones, transport proteins, and antibodies employ receptormediated endocytosis to gain entry into a cell. A less advantageous consequence is that this pathway is available to viruses and toxins as a means of entry into cells. The reverse process—the fusion of a vesicle to a membrane—is a key step in the release of neurotransmitters from a neuron into the synaptic cleft (Figure 12.41). Although the processes of budding and fusion appear deceptively simple, the structures of the intermediates in the budding and fusing processes and the detailed mechanisms remain active areas of investigation.

Figure 12.41. Neurotransmitter Release.

Figure 12.41

Neurotransmitter Release. Neurotransmitter-containing synaptic vesicles are arrayed near the plasma membrane of a nerve cell. Synaptic vesicles fuse with the plasma membrane, releasing the neurotransmitter into the synaptic cleft. [T. Reese/Don Fawcett/ (more...)

By agreement with the publisher, this book is accessible by the search feature, but cannot be browsed.

Copyright © 2002, W. H. Freeman and Company.
Bookshelf ID: NBK22465

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