Specific amino acid sequence deciding where proteins target

Some are part of the protein permanent signal peptides are located in N, C or middle of the protein Some proteins have more than one signal

Sequence, charge, length

Outer membrane, innermembrane, intermembranous space

Integral proteins that transport proteins

Keep proteins unfolded

help guide the newly created protein cross the pore

Hsp70 releases the protein and then quickly replace the used ATP

Inner potential and ATP breaking

Attracts the +charged presequence into the matrix

Membrane-enclosed organelle containing many oxidative enzymes without DNA or ribosomes

PTS1, PTS2

At C terminus with 3 conserved amino acids

In N-terminus with loose consensus

Lipids made in the er

Insert proteins into the peroxisomal membrane

PEX3 and 16, PEX5, PEX7

Import of membrane protein

Import of type1 protein into peroxisome matrix

Import of type2 protein into peroxisome matrix

16,456 bp with only 13 mitochondrial membrane protein, 2 ribosomal RNAs and some essential tRNA

Increase surface area for ATP creation

3 folds larger

Use the transport of high energy electron to create gradient of proteins in inner membrane

Divide and fuse

Number of mitochondria

Leads to small mitochondria and defects in the myelin sheath that insulates axons

Getting most of its protein from cytoplasm while making some of its own internally replicating their DNA

Glycolysis, fatty acid oxidation

Generate Acetyl-CoA to feed the citric acid cycle

Drive electron transport pathway in the inner mitochondria membrane

Electrochemical gradient of protons drives ATP creation

Process of making new mitochondria

Refers to how well mitochondria makes energy

Biggest part of the cell that is enclosed by a membrane

Expansion of prokaryotic plasma membrane

• Most important source of lipid • Form the nuclear envelope • Lumen of ER is the major place for protein creation and folding

Process where protein is made and folded at the same time at ER with the help of SRP

Where only protein folding is done in the er

Attach to newly made proteins to keep unfolded until they bind to Sec63

ER by signal sequencing and will be cleaved by signal peptidase

C-terminus in the cytoplasm.

N-terminus in the cytoplasm.

Interact with the bilayer by a single stretch of hydrophobic amino acids at the C-terminus.

Single protein chain turning into a specific shape

Multiple protein chains linking together to form a larger protein complex

process of breaking down proteins into smaller pieces, misfolded proteins are removed or fixed

SREBP

Proteins made in the cytoplasm are tagged and transported to mitochondria to be refolded.

Proteins going to peroxisomes are created in the cytoplasm, tagged with a special tag, and directly transported into the peroxisome without unfolding.

Mitochondria grow and divide within cells, they get most of their proteins from the cytoplasm while making some of its own protein internally replicating their DNA.

Proteins are made and moved around the cell using systems of membrane often are modified

Proteins destined for the ER are made directly to go the the ER,After they are in they fold

During translation, if the protein carries an ER signal sequence, SRP halts translation, guiding the ribosome to the ER membrane where the protein is inserted.

Proteins with ER signal go to ER; those without stay in cytosol.

Proteins with a (NLS) are transported through nuclear pores to the nucleus

Proteins destined for mitochondria, chloroplasts, and peroxisomes are transported across their membranes.

Proteins for the ER, Golgi, lysosomes, and cell membrane are carried by vesicles