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Flow of genetic information in all living cells
DNA -> RNA -> Protein
Replication-> Transcription -> Translation
Miller-Urey experiment
recreated conditions thought to exist in the atmosphere of primitive earth. No Oxygen!
Used heat to simulate sun, electric discharge to simulate lightning, and cooling to condense molecules to liquid form.
7 simple molecules: water vapor, nitrogen, ammonia, co2, co, methane, and hydrogen.
Miller-Urey results
With each round of heating, energy radiation, and cooling, more complex organisms were formed:
1. aldehydes
2. simple acids
3. more complex acids
Suggests organic molecules can form under abiotic conditions.
Ribozome catalyzed reactions
observed in:
genome replication in some RNA viruses
intron splicing
ribosome function in translation
Evidence for RNA World
RNA can catalyze the polymerization of nucleotides, including the synthesis of complementary RNA, using itself as a template. Not observed in DNA.
The first cell
self-replicating RNA and other life-promoting molecules inside a phospholipid membrane
What Constrains the size of a cell?
The ratio of surface area to volume. Smaller cells have a greater surface area to volume ratio.
Surface area to volume ratio
radius = 1cm -> Surface area : volume ratio is ~ 3:1
Radius = 10cm -> Suface area : volume ratio is ~ 1:3
High sa : v ratio means
more membrane per unite of volume. important for the cell to interact with its environment. smaller cell interact more efficiently; less likely to lose energy as heat to surroundings.
prokaryotic cell
no nucleus
no organelles
single chromosome (in nucleoid area) +plasmids
cell wall
capsule
most diverse of cells
Photosynthetic bacteria
obtain energy from sunlight. have internal system of membranes where photosynthesis occurs.
chemosynthetic
derive energy from oxidation of H2S.
ex. Filamentous Beggiatoa
Mitochondria
organelles found in most eukaryotic cells and generate most of the cell's supply of usable energy. extract energy from food
DNA-containing organelles (endosymbionts)
enclosed by double membrane
chloroplasts
organelles found in plant cells and ukaryotic algae. harvest energy from sunlight by photosynthesis.
DNA-containing organelles
larger than mitochondria
two membranes + a 3rd membrane system, the thylakoid.
thylakoid
contains the photosynthetic pigment chlorophyll
endocytosis
import mediated by the formation of endocytic vesicles
exocytosis
export
endosymbiosis
mitochondria and chloroplasts were prokaryotes that entered eukaryotic cells and became specialized to perform specific cellular functions
Evidence of endosymbiosis
resemble present-day prokaryotes in size
-organelles contain their own DNA (organelle genomes)
-organelle genomic sequences resemble those of present-day prokaryotes
-organelles can divide independent of mitosis and cell division
-organelles are enclosed by double membranes
Animal cell
nucleus
chromosomes
mitochondria
centrioles (microtubule organizing center)
no cell wall
Plant cell
nucleus
chromosomes
mitochondria
chloroplasts
no centrioles
microtubule organizing center (but no centrioles)
large vacuoles (fluid filled compartments)
cell wall
Animal cell types
epithelial, connective tissues, blood cells, neurons, muscle cells
epithelial cells
cells are bound by tight junctions and form sheets that cover body surfaces and form the lining of internal organs (e.g. mouth, bile duct, intestine)
connective tissues
bone and cartilage
adipose tissue
fibroblasts
blood cell types
red (O2 transport)
white (immune)
neurons
cells that receive and transmit signals throughout the body and are capable of generating electrical activity
Muscle cells
multi-nucleated cells that generate force and movement.
three types:
skeletal
cardiac
smooth
Basic properties of cells
complexity
genetics
replication
metabolism
biochemistry
function
response
self-regulation
complexity
cells are highly complex and organized
genetics
cells possess a genetic program and the means to use it
replication
cells are capable of producing more of themselves
metabolism
cells are capable of acquiring and utilizing energy
biochemistry
cells carry out a variety of chemical reactions
function
cells engage in numerous mechanical activities
response
cells are able to respond to external stimuli
self-regulation
cells maintain their complex state by constant self-regulation
building blocks of the cell
sugars
fatty acids
amino acids
nucleotides
larger units of the cell
polysaccharides
fats, lipids, membranes
proteins
nucleic acids
sugars
polysaccharides
fatty acids
fats, lipids, membranes
amino acids
proteins
nucleotides
nucleic acids
ribonucleosides or deoxyribonucleosides + phosphates
formation of macromolecules by condensation reactions
subunits are added to one end of a growing chain by dehydration synthesis
formation of disaccharides
the condensation of two monosaccharides produces one disaccharide
reverse reaction of condensation
hydrolysis (water consumed instead of being expelled)
carboxylic acid head
hydrophilic
hydrocarbon tail
hydrophobic
triaglycerols
formed when fatty acids stored as energy reserves (fats and oils) through an ester linkage to glycerol
saturated fatty acids
tend to form aggregates and deposits within the walls of blood vessels causing atherosclerosis of coronary blood vessels (coronary heart disease)
Cis unsaturated fatty acids
cis unsaturated fatty acids do not form solid aggregates
e.g. oleic acid (comprises 80% of olive oil)
Trans unsaturated fatty acids
behave similar to saturated fatty acids = they tend to aggregate and form solid deposits.
e.g. elaidic acid (found in partially hydrogenated vegetable oils)
phospholipids
in biological membranes typically contain one saturated and one unsaturated fatty acid.
saturated fatty acid makes the membrane less fluid because they tend to aggregate.
cis unsaturated fatty acids reduce membrane rigidity because they do not form solid aggregates.
alanine
one of the simplest amino acids
polypeptide
held together with peptide bonds. N-terminus capped by amino group and C-terminus capped by carboxyl group
Adenosine triphosphate
a nucleotide. ATP. used as an energy carrier in the cell
Ribonucleosides
Guanosine
Adenosine
Cytidine
Uridine
Deoxyribonucleosides
deoxyguanosine
deoxyadenosine
deoxycytidine
deoxythymidine
cyclic adenosine monosphosphate
cAMP. a cyclic nucleotide
Relative abundance of macromolecules in cells
30% chemicals:
DNA (1%)
polysaccharides (2%)
phospholipids (2%)
ions, small molecules (4%)
proteins (15%)
70% water
formed from the covalent bonding of their monomeric subunits
polysaccharides, polypeptides, and polynucleotides
interactions between macromolecules
mediated by noncovalent bonds of compatible groups. results in macromolecular complexes in cells.
e.g. molecule A randomly encounters other molecules (B,C, D). Surfaces of molecules B and C do not match A. A few weak bonds are formed but thermal motion breaks them apart. Surface of D matches Surface of A. Forms a lot of weak bonds that are able to withstand thermal jolting.
nonpolar side chains
tend to cluster at the interior of a folded polypeptide, away from the aqueous surroundings. also form the transmembrane domains of membrane proteins.
polar and charged amino acids
tend to be near the outside of the protein, the surface exposed to the aqueous surroundings.
globular protein
(folded conformation in aqueous environment)
hydrophobic core region (contains nonpolar side chains)
hydrogen bonds can be formed to the polar side chains on the outside of the molecule.
alpha helix
polypeptide structure. each N-H is bonded to the C=O of a neighboring peptide bond located four amino acids away in the same chain.
Beta sheet
polypeptide structure. individual polypeptide chains in each sheet are held together by hydrogen bonding between peptide bonds in different strands, and the amino acid side chains in each strand project alternately above and below the plane of the sheet.
protein maturation involves:
correct folding
proteolytic cleavage
chemical modifications
formation of quaternary structures
association with co-factors
protein regulation
each step in protein synthesis and maturation can be a target for regulation of protein function.
protein degradation
under tight control
chaperones
bind to nascent polypeptides and maintain a stable unfolded state. when synthesis is complete, the polypeptide is released and allowed to fold correctly.
if a protein is to be transported through a membrane:
1) chaperones stabilize the newly synthesized polypeptide.
2) the polypeptide is transported
3) chaperones on the other side maintain the unfolded state until translocation is complete
4) only then is the polypeptide allowed to fold into 3D shape
cross-linking
disulfide bonds form between adjacent cysteine residues.
they can link two domains of the same polypeptide or different polypeptide chains
denaturants
can unfold (denature) a polypeptide by breaking noncovalent interactions between amino acids. (e.g. urea or heat)
reducing agents
can break disulfide bonds. (e.g. beta-mercaptoethanol)
urea
produced in the liver of mammals as a way to excrete ammonia (a toxic metabolic waste product). can reversibly break noncovalent interactions between amino acids.
fibrillar collagens
the major structural proteins of connective tissues. build of triple helices of procollagen polypeptides.
prions
proteinaceous infectious particle. infectious agent.
protein-only hypothesis
diseases are caused by incorrectly folded versions of the prion protein
TSE
family of fatal brain diseases characterized by lesions that appear as small cavities (spongy appearance) caused by protein aggregates
Regulation of gene expression
determines the amount of protein produced by the cell by limiting transcription and/or translation
regulation of protein function
the protein is synthesized but its activity is restricted according to needs of the cell.
PKA
protein kinase A. promotes glycogen metabolism. cAMP activates PKA by binding to the regulatory subunits, causing the release of the catalytic subunits. the kinase activity of the released catalytic subunits phosphorylate multiple effector proteins
feedback inhibition
the end product of a biosynthetic pathway inhibits the enzyme that catalyzes the first step, causing the entire pathway to shut down.
allosteric regulation
a change in the conformation of a protein that affects its activity due to the binding of a regulatory molecule.
regulation of glucose metabolism
enzyme activity responds to elevated ADP levels
protein kinases
enzymes that transfer a phosphate group from ATP to proteins
two types of kinases
1. serine/threonine
2. tyrosine
phosphatases
enzymes that remove phosphate groups from phosphorylated proteins.
ubiquitin
a small protein that is attached to a target protein as a label for regulation or destruction
ubiquitylation and proteasomal degredation
1) target protein has several ubiquitins attached by ubiquitin ligase enzyme.
2) a cap domain of the proteasome recognizes the polyubiuitylated target protein
3) the ubiquitins are removed and recycled
4) the proteasome degrades the target protein by sequential ATP-dependent steps.
centromere
the point of junction between sister chromatids. also the attachment site for mitotic spindle proteins.
telomeres
the stable ends of linear chromosomes
replication origins
sequences where DNA replication begins
levels of organization of DNA in chromosomes:
1) nucleosomes
2) chromatin
3) chromatin fibers
4) condensed chromosomes
condensed chromosome
highest level of DNA organization.
ATP dependent enzyme complexes
can displace nucleosomal dna to expose specific sequences that can then be recognized by DNA-binding proteins
chromatin remodeling complexes
use energy from ATP hydrolysis to push the histone-bound DNA along the histone core, thereby exposing the underlying DNA.
emrbyonic stem cells
capable of becoming any type of cell because they have not undergone any differentiation
(totipotent)
adult stem cells
have limitations on which cell types they are capable of becoming because they have under-gone some differentiation (pluripotent)
e.g. blood stem cells
terminally differentiated cell types
can not become any other cell type (neurons, muscle cells, endocrine cells, blood cells, etc)