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Other forms of processing of cytosolic proteins involve

Glycosylation. Most proteins are modified in the endoplasmic reticulum by addition of polysaccharides. This process is called . The enzymes that carry out these reactions are located in the lumen of the ER and not in the cytosol. This means that the proteins being glycosylated are bound for secretion or are membrane proteins.

The transient proteins stay in place and enjoy the ride. Accounting for the resident proteins is the hard part. We have to assume that the resident proteins have targeting signals that allow them to be sorted and concentrated into vesicles and shipped back to where they belong, via retrograde vesicle transport in the direction.

Rough ER has ribosomes on the cytosolic surface.

Therefore, the rest of the polypeptide remains on the cytosolic side.

All protein synthesis begins on ribosomes in the cytosol which are unattached to the ER ().

The oligosaccharide chain is attached to an residue through its free amino group. The asparagine residue is part of a three- amino acid target sequence consisting of asparagine, any amino acid followed by serine or threonine. The enzyme that transfers the oligosaccharide to the protein is called oligosccharide protein glycosyl transferase (this will not be on the exam).

The cells were collected and suspended in hypotonicbuffer [10 mM HEPES, pH 7.9, 1.5 mM MgCl, 10 mMpotassium chloride (KCl), 0.2 mM PMSF, 0.5 mM dithiothreitol (DTT)and 10 μg/ml aprotinin], after which they were incubated on ice for10 min. The cells were then lysed by the addition of 0.1% NonidetP-40 and vigorous vortexing for 10 sec. The cells were thencentrifuged at 4,000 rpm for 5 min at 4°C, after which thesupernatants containing protein were collected. The pelletsacquired from the cytosolic protein extraction were thenresuspended in high salt buffer (20 mM HEPES, pH 7.9, 25% glycerol,400 mM KCl, 1.5 mM MgCl, 0.2 mM EDTA, 0.5 mM DTT, 1 mMNaF and 1 mM sodium orthovanadate). Finally, the cells werecentrifuged at 14,000 rpm for 5 min at 4°C, and the supernatantswere stored.

The receptor may be located in the cytosol or in the nucleus.

These transport vesicles bud from the periphery of the Golgi cisterna as shown in the picture , and then fuse with the appropriate target cisterna ( to the point of origin) via the normal vesicle targeting process. In this manner a transient protein makes is way down the Golgi stack, to .

The amines are stored in cytosolic vesicles until their release is triggered.

The cytosol has a high gluathione concentration, which
makes it a reducing environment, and so proteins with disulphide bridges (-S-S-) can not be made here (since the disulphide bridge
would remain reduced to hydrogen sulphide groups (-SH + HS-).

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Binding of Ca++ with protein in the cytosol, and


Spliceosomes occur in both the nucleus and cytosol.

The construction of the proteins is carried out on the of the host . There are free floating ribosomes where proteins are built for functions in the cytoplasm. Those proteins which are to be used as part of the cell membrane or transported outside the cell are manufactured on ribosomes which are attached to the .

A cytosolic protein catalyzes the release of GDP ..

Background - Heat shock proteins (HSPs) are well known for their ability to "protect" the structure and function of native macromolecules, particularly as they traffic across membranes. Considering the role of key mitochondrial proteins in apoptosis and the known antiapoptotic effects of HSP27 and HSP72, we postulated that HSP60, primarily a mitochondrial protein, also exerts an antiapoptotic effect. Methods and Results - To test this hypothesis, we used an antisense phosphorothioate oligonucleotide to effect a 50% reduction in the levels of HSP60 in cardiac myocytes, a cell type that has abundant mitochondria. The induced decrease in HSP60 precipitated apoptosis, as manifested by the release of cytochrome c, activation of caspase 3, and induction of DNA fragmentation. Antisense treatment was associated with an increase in bax and a decrease in bcl-2 secondary to increased synthesis of bax and degradation of bcl-2. A control oligonucleotide had no effect on these measurements. We further demonstrated that cytosolic HSP60 forms a macromolecular complex with bax and bak in vitro suggesting that complex formation with HSP60 may block the ability of bax and bak to effect apoptosis in vivo. Lastly, we show that as cytosolic (nonmitochondrial) HSP60 decreases, a small unbound fraction of bax appears and that the amount of bax associated with the mitochondria and cell membranes increases. Conclusions - These results support a key antiapoptotic role for cytosolic HSP60. To our knowledge, this is the first report suggesting that interactions of HSP60 with bax and/or bak regulate apoptosis.

Cytosolic Protein Phosphatases | Thoracic Key

N2 - Background - Heat shock proteins (HSPs) are well known for their ability to "protect" the structure and function of native macromolecules, particularly as they traffic across membranes. Considering the role of key mitochondrial proteins in apoptosis and the known antiapoptotic effects of HSP27 and HSP72, we postulated that HSP60, primarily a mitochondrial protein, also exerts an antiapoptotic effect. Methods and Results - To test this hypothesis, we used an antisense phosphorothioate oligonucleotide to effect a 50% reduction in the levels of HSP60 in cardiac myocytes, a cell type that has abundant mitochondria. The induced decrease in HSP60 precipitated apoptosis, as manifested by the release of cytochrome c, activation of caspase 3, and induction of DNA fragmentation. Antisense treatment was associated with an increase in bax and a decrease in bcl-2 secondary to increased synthesis of bax and degradation of bcl-2. A control oligonucleotide had no effect on these measurements. We further demonstrated that cytosolic HSP60 forms a macromolecular complex with bax and bak in vitro suggesting that complex formation with HSP60 may block the ability of bax and bak to effect apoptosis in vivo. Lastly, we show that as cytosolic (nonmitochondrial) HSP60 decreases, a small unbound fraction of bax appears and that the amount of bax associated with the mitochondria and cell membranes increases. Conclusions - These results support a key antiapoptotic role for cytosolic HSP60. To our knowledge, this is the first report suggesting that interactions of HSP60 with bax and/or bak regulate apoptosis.

The term "cytosol" was first introduced in 1965 by H

AB - Background - Heat shock proteins (HSPs) are well known for their ability to "protect" the structure and function of native macromolecules, particularly as they traffic across membranes. Considering the role of key mitochondrial proteins in apoptosis and the known antiapoptotic effects of HSP27 and HSP72, we postulated that HSP60, primarily a mitochondrial protein, also exerts an antiapoptotic effect. Methods and Results - To test this hypothesis, we used an antisense phosphorothioate oligonucleotide to effect a 50% reduction in the levels of HSP60 in cardiac myocytes, a cell type that has abundant mitochondria. The induced decrease in HSP60 precipitated apoptosis, as manifested by the release of cytochrome c, activation of caspase 3, and induction of DNA fragmentation. Antisense treatment was associated with an increase in bax and a decrease in bcl-2 secondary to increased synthesis of bax and degradation of bcl-2. A control oligonucleotide had no effect on these measurements. We further demonstrated that cytosolic HSP60 forms a macromolecular complex with bax and bak in vitro suggesting that complex formation with HSP60 may block the ability of bax and bak to effect apoptosis in vivo. Lastly, we show that as cytosolic (nonmitochondrial) HSP60 decreases, a small unbound fraction of bax appears and that the amount of bax associated with the mitochondria and cell membranes increases. Conclusions - These results support a key antiapoptotic role for cytosolic HSP60. To our knowledge, this is the first report suggesting that interactions of HSP60 with bax and/or bak regulate apoptosis.

(Cytosolic, Calcium-Dependent) Protein 120 anti ..

The process of translation can be divided into the stages of initiation, elongation, and termination. Initiation involves at least three other proteins called initiation factors to help bind the mRNA to the smaller subunit of the two-unit ribosome. It is bound to the correct location using the initiation codon AUG on the mRNA. The next phase is elongation, or adding other amino acids to the building polypeptide chain. According to Karp, a step of elongation can be accomplished in about 1/20 second, so a small protein of 400 units could be assembled in about 20 seconds! It is suggested that most of this time is used sampling the amino-acid-carrying tRNAs in the cytosol to find the ones for which there is a codon-anticodon match for the next codon along the mRNA pattern.

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