Flashcards in Organelles I Deck (39):
Formation of Eukaryotes
Endosymbiosis of eubacteria with archeabacteria
Function as pores and receptors
Peripheral membrane proteins
Accessory proteins to the function of transmembrane proteins.
Act through a signal transduction pathway
Saccharides on Cell Membrane
attach to the lipid (glycolipid) or proteins (glycoproteins)
Space between the inner and outer nuclear membranes
have nuclear export and import localization sequences which bind specifically to transport proteins that in turn interact with proteins of the pore complex for transfer across the nuclear envelope
- Active Transport. Big Molecules
Makes Ribosomal RNA
- Conssit of DNA sequences coding for rRNA
Consists of primary rRNA transcripts
Mature ribosomal subunits
The pars fibrosa and pars granulosa.
Excludes pars amorpha
Heavy Staining, show up dark.
Plant Nucleotide Pairs
They have a lot more DNA due to the ability to perform photosynthesis.
Also, plants are sedentary and need genes that transcript for survival mechanisms.
Amphibian Nucleotide Pairs
They have a lot genes because of their two lifestyles: Land and water
Period of growth between mitosis. G1, S, G2.
nucleus disappears and chromatin condense into chromosomes. Centrosomes migrate to opposite poles. Mitotic spindle forms
chromosomes further condense and align at the equatorial plane
sister chromosomes move toward spindle poles
sister chromsomes arrive at the poles
cleavage furrow divides the cytoplasm and duplicated chromsomes into two daughter cells.
consist of a small and large subunit that come together by binding a mRNA strand.
Translation of proteins
synthesize proteins that stay in the cell
Rough ER Ribosomes
synthesize proteins that are secreted out of the cell
Functions of ER
1. Cleavage of signal peptide
2. Protein folding
3. Attachment of oligosaccharides
4. Smooth ER synthesize phospholipids, fats, and steroids
5. Enzymes responsible for detoxification of drugs and other harmful substances
Protein Folding in the RER
1. Signal peptide is cleaved off
2. Polypeptide is pushed into lumen of ER with chaperone proteins
3. Proper folding and posttranslational modifications occur
4. Misfolded proteins are translocated into cytosol and degraded.
Saccharide moieties are transferred onto polypeptide chain from glycoproteins
Stack of membranes in the cell that modifies, sorts and packages proteins from the ER.
- Continuous with the ER
- Cis face is closest to RER
- Trans face releases large vesicles with mature proteins
Protein that promotes forward movement from ER to Golgi
Protein that promotes retrograde movement of vesicles from Golgi to ER
mediates the retrieval of misfolded proteins from the Golgi back to the ER
cis Golgi Network
phosphorylation of oligosaccharides on lysosomal proteins
removal of mannose
removal of mannose and addition of n-acetylglucosamine
addition of galactose
trans Golgi Network
Addition of n-acetylneutraminic acid NANA
Marker that is added during cis Golgi that determines segregation to lysosomes
- bind with other vesicles and create an acidic envirnoment
- acid hydrolases exhibit optimal enzymatic activity at pH 5