Passageway for molecules into and out of the nucleus.
Where most of the genetic material is organized and expressed.
Double membrane that encloses the nucleus.
Site where macromolecules are degraded.
Site for ribosome subunit assembly.
A complex of protein and DNA.
Site of polypeptide synthesis.
Membrane that controls movement of substances into and out of the cell; site of cell signaling.
Site of many metabolic pathways.
Site of modification, sorting, and secretion of lipids and proteins. Packages materials into SECRETORY vesicle.
Site where hydrogen peroxide and other harmful molecules are broken down.
Protein filaments that provide shape and aid in movement.
Site of ATP synthesis. Involved in the synthesis, modificiation and breakdown of several types of cell brown fat cells. Generate heat known as brown fat cells which serve as "heating pads" that help to revive hibernating animals and protects us.
Site of detoxification and lipid synthesis.
Site of protein sorting and secretion
PLANT CELL, Site of photosynthesis
PLANT CELL, Site that provides storage; regulation of cell volume.
PLANT CELL, Structure that provides cell support.
PROKARYOTES, Allow certain bacteria to swim.
PROKARYOTES, Allow bacteria to attach to surfaces and to each other.
PROKARYOTES, Site where the DNA is found
PROKARYOTES, Outer glatinous covering. Traps water andhelps protect bacteria form drying out.
PROKARYOTES, A thick, gelatinous glycocalyx that helps them avoid being destroyed by the animal's immune system or aid in the attachment to cell surfaces.
Includes Nuclear envelope, endoplasmic reticulum, Golgi Apparatus, Lysosomes, vacuoles, plasma membrane and peroxisomes
The internal structure shared by flagella and cilia. Contains microtubules, the motor protein dynein, and linking proteins. Microtubules form an arrangement called a 9+2 array.
Tow parts: the nuclear lamina (intermediate filaments that line the inner nuclear membrane) and the internal nuclear matrix.
Serves to organize the chromosomes within the nucleus
A network of membranes that form the form flattened, fluid-filled tubules of the Endoplasmic Reticulum.
The internal space of an organelle.
Entire route where Proteins destined for secretion are synthesized into the ER, travel to the Golgi, and then are transported by vesicles.
In Plant seeds, Enzymes that are needed to convert fats to sugars.
Mitochondria and chloroplasts. They can grow and divide to reproduce themselves, but they are not completely autonomous because they depend on other parts of the cell for their internal components.
A third system of membranes, forms many flattened fluid-filled tubules that enclose a single convoluted compartment within a chloroplast.
The tubules stacked on top of each other in chloroplasts
The compartment of the chloroplast that is enclosed by the inner membrane but outside the thykaloid membrane.
Chloroplasts Chromoplasts: synthesize and store the yellow, orange and red pigments known as carotenoids. Give fall leaves their color. Leucoplasts: Lack pigment Amyloplast: A leucoplast that synthesizes and stores starch. Common in roots and tubers.
When the synthesis of a protein is halted until the ribosome is bound to the ER membrane. Sorting process begins while translation is occuring.
Cotranslational Sorting of Protein @ER
1. Polypeptide contains an ER signal sequence 2. ER signal sequence recognized by a protein called signal recognition particle (SRP.) 3. SRP pauses translation, binds to a recepton in ER and docks ribosome over a channel protein. 4.SRP leaves and polypeptide threaded through channel to cross ER membrane; ER signal sequence removed by signal peptidase.
Vesicle Formation of Proteins
1. Vesicle formation facilitated by coat proteins. 2.When vesicle buds from membrane, v-snares incorporated into the vesicle membrane. 3. Vesicle released, coat is shed, v-snares in membrane are recognized by t-snares in target membrane. 4. Vesicle fuses with membrane containing the t-snares.
Post-translational protein sorting to nucleus, peroxisome, mitochondria and chloroplasts
1.Chaperone proteins keep protein unfolded. 2. Matrix-targeting sequence binds to receptor. 3. Chaperones are released as protein is transferred to a channel in the outer membrane. 4.Protein is transfered to a channel in the inner membrane. 5.Chaperones bind to protein as it enters the matrix. 6.Matrix-targeting sequence cleaved by enzyme. 7.Protein is completely threaded into the matrix 8. Chaperones are released, and protein folds into its 3-D shape.
4 Interacting parts of a Eukaryotic Cell
the interior of the nucleus the cytosol the endomembrane system the semi-autonomous organelles
Component of a Phospholipid
2 fatty acids w/acyl tail 1 glycerol 1 Phosphate 1 Polar Head Group
Occurs in Archaea Carbohydrate attached to the amino acid asparagine in polypeptide chain 1.Group of 14 sugar molecules built onto a lipid called dolichol 2. Carb. tree transferred to asparagine, peptide synthesized into ER lumen through a channel protein. 3. An ER enzyme, oligosaccharide transferase, recognizes sequence and transfers carb tree form dolichol to asparagine
Occurs in the Golgi apparatus Involves the addition of a string of sugars to oxygen atom of serine or threonine Important for production of proteoglycans (highly glycosylated proteins that are secreted from cells and help to organize the extracellular matrix)
High permeability through bilayer
Gases Very small, uncharged molecules (Ethanol)
Moderate permeability through bilayer
Low permeability through bilayer
Polar organic molecules (sugars)
Very low permeability through bilayer
Ions Charged polar molecules and macromolecules
When water exits the cell and the plasma membrane pulls away from the cell wall
When a cell takes up so much water it ruptures
When water exits the cells causing them to shrink.
Degradation of mRNA: 1. Tail removed 2. 5'cap removed 3. Removes nucleotides starting at the 5' end and moving toward the 3' end.
Degradation of mRNA: 1. Tail removed 2. RNA degraded in 3' to 5' direction via the exosome.
Break Down Protein in Proteasome
1.String of ubiquitns attached to a target protein. 2.Protein w/ubiquitin directed to the proteasome. 3.Protein is unfolded by enzymes in the cap and injected into the core proteasome. Ubiquitin released back into the cytosol. 4.Protein is degraded to small peptides and amino acids. 5.Small peptides and amino acids are recycled back to the cytosol.
Cytoplasm v.s. Cytosol
Cytoplasm=region enclosed by the plasma membrane, includes they cytosol and organelles Cytosol=region of cell outside membrane-bound organelles but inside the plasma membrane
Smooth ER Liver Cells
Enzymes in smoother ER of liver detoxify evil molecules, convert hydrophobic toxic molecules into hydrophilic molecules, excreted from body
Provides surface area for enzymes in metabolic roles (liver cells) Carbohydrate metabolism Accumulation of Ca2+ ions Synthesis of phospholipids and lipids (like cholesterol, which makes testosterone and estrogen)
Sorts proteins Inserts proteins into the ER Attaches carbs to proteins and lipids (Glycosylation)
attaching carbs to proteins and lipids
Processing Protein sorting Secretion Glycosylationq
Enzymes called proteases cut proteins into smaller polypeptides In golgi apparatus
Found in animal cells, lyse macromolecules Contain acid hydrolases that break down carbs, proteins, lipids and nucleic acids Break down stuff from endocytosis
Break down molecules to make new ones
Fluid-filled lumen Breakdown molecules by removing H or adding O makes hydrogen peroxide H2O2<-- use catalase enzym to break down to H20 and O2
Cell adhesion Membrane transport Cell signaling
Cisternae VS Cristae
Cisternae = the folded membranes of the ER Cristae = the folded membranes of the Mitochondria