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MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor
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MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

Dec 21, 2015

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Page 1: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

MOLECULAR CHAPERONES

The Department of Biochemistryof Medical Faculty

Presents now

Edited by Attila Sandor

Page 2: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

three dimensional informationone dimensional information

L. Fig.3-16, p.89

Page 3: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

Str., Fig. 7.1, p.172

The model proteins for classic study of developing the three dimensional structure, that for folding. (Anfinsen)

Page 4: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

Str. Fig. 3.53, p. 65

Page 5: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

Scrambled

Str. Fig. 3.54, p. 66

Page 6: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

The three dimensional structure is dictated entirely by the amino acid sequence

Str., Fig1.6 p.7

Page 7: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

L.Fig.4-29,p. 149

Fre

e en

ergy

Page 8: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

Str. Fig. 3.57, p. 6+8

Page 9: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

(a) The folding of the unfolded protein (U) to the correct (C) form is favored thermodynamically. Chaperone is not necessary.

(b) The folding of the unfolded protein (U) to the incorrect (I) form is favored thermodynamically. Chaperone is necessary.

Role of chaperones in the thermodynamic point of view

Ellis R.J., Annu. Rev. Biochem., 1991

Page 10: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

The idea of molecular chaperones

Named after the human chaperone: “usually an elderly woman who accompanies a young unmarried lady to prevent not proper interactions

with other people.

Molecular chaperones: proteins assisting folding of nascent polypeptides, by preventing wrong folding.

Molecular chaperones catalyze the formation of correctly folded, functionally active, native proteins, but they are not part of the product.

Expression of many chaperon is induced by stress, such as by heat, because during heat-stress the probability of wrong folding is higher, therefore cells need more protection.

These chaperons are called heat shock proteins (HSP’s).

Author`s slide

Page 11: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

Representative members of the Chaperone family

Nucleoplasmins

Chaperonins

Heat shock proteins 70( Hsp70)

NucloplasminNucleoplasminS

chaperonin 60, groELchaperonin 60, groELchaperonin 10, groES(mitochondrial, bacterial)may use ATP

Heat shock proteins 90 (Hsp90)

Ellis R.J., Annu. Rev. Biochem., 1991

Page 12: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

DNA + Histone aggregate

DNA+ Nucleoplasmin + Histone Nucleosoma (DNA + Histone)

Nucleoplasmin

Role of nucleoplasmines: assably of chromatin

Author`s picture

Page 13: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

Representative members of the Chaperone family

Nucleoplasmins

Chaperonins

Heat shock proteins 70( Hsp70)

NucloplasminNucleoplasminS

chaperonin 60, groELchaperonin 60, groELchaperonin 10, groES(mitochondrial, bacterial)may use ATP

Heat shock proteins 90 (Hsp90)

Ellis R.J., Annu. Rev. Biochem., 1991

Page 14: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

Rubisco denaturated with guanine at +10o C

RUBISCO and the chaperonins

Rubisco denaturated with guanine at +25o Cand chaperonin 60, chaperonin 10, ATP, Mg++ were added

When removing guanine

very poor recovery

80% recovery

Rubisco denaturated with guanine at +25o C

good recovery

Rubisco: ribulose 1,5-bisphosphate carboxylase-oxygenase

Author`s slide

Page 15: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

L.Fig.41-31, p.152

Page 16: MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor.

THANK YOU FOR YOUR ATTENTION

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Attila Sandor

c:\sandor\chaperon.ppt