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Subunit Mobility and the Chaperone Activity of Recombinant alphaB-Crystallin.

Krushelnitsky A, Mukhametshina N, Gogolev Y, Tarasova N, Faizullin D, Zinkevich T, Gnezdilov O, Fedotov V - Open Biochem J (2008)

Bottom Line: The comparison of the chaperone-like activity of native and covalently cross-linked human alphaB-crystallins has confirmed the important role of the subunit mobility in the chaperoning mechanism.Our data clearly demonstrate that the chaperone-like activity of alpha-crystallin is not only a surface phenomenon as was suggested by some researchers.

View Article: PubMed Central - PubMed

Affiliation: Kazan Institute of Biochemistry and Biophysics, Russian Academy of Sciences, Kazan, Russia.

ABSTRACT
The comparison of the chaperone-like activity of native and covalently cross-linked human alphaB-crystallins has confirmed the important role of the subunit mobility in the chaperoning mechanism. Our data clearly demonstrate that the chaperone-like activity of alpha-crystallin is not only a surface phenomenon as was suggested by some researchers.

No MeSH data available.


The Amide I band of the infra-red spectra of the native and cross-linked αB-crystallin. The spectra were normalized to the integral intensity of the Amide I band
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Figure 2: The Amide I band of the infra-red spectra of the native and cross-linked αB-crystallin. The spectra were normalized to the integral intensity of the Amide I band

Mentions: To relate the difference in the chaperone-like activity between native and cross-linked αB-crystallins solely to the subunit mobility effect, one has to exclude other possible reasons of such a difference. Namely, cross-linking should not lead to the change of the protein structure and appearance of inter-molecular (i.e. inter-aggregate) cross-links. The size of the cross-linked aggregates was checked by Augusteyn by means of the gel permeation chromatography [17]. In our work, we used other experimental techniques to present an independent proof that cross-linking does not change α-crystallin properties, except subunit mobility. We have recorded IR spectra and measured translational SDC of the native and cross-linked αB-crystallins. Fig. (2) presents IR spectra of the Amide I peak that is very sensitive to the protein secondary structure composition. It is seen that native and cross-linked proteins reveal no secondary structure differences. Hence, the structural effect on the chaperone-like activity can be ruled out.


Subunit Mobility and the Chaperone Activity of Recombinant alphaB-Crystallin.

Krushelnitsky A, Mukhametshina N, Gogolev Y, Tarasova N, Faizullin D, Zinkevich T, Gnezdilov O, Fedotov V - Open Biochem J (2008)

The Amide I band of the infra-red spectra of the native and cross-linked αB-crystallin. The spectra were normalized to the integral intensity of the Amide I band
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2570560&req=5

Figure 2: The Amide I band of the infra-red spectra of the native and cross-linked αB-crystallin. The spectra were normalized to the integral intensity of the Amide I band
Mentions: To relate the difference in the chaperone-like activity between native and cross-linked αB-crystallins solely to the subunit mobility effect, one has to exclude other possible reasons of such a difference. Namely, cross-linking should not lead to the change of the protein structure and appearance of inter-molecular (i.e. inter-aggregate) cross-links. The size of the cross-linked aggregates was checked by Augusteyn by means of the gel permeation chromatography [17]. In our work, we used other experimental techniques to present an independent proof that cross-linking does not change α-crystallin properties, except subunit mobility. We have recorded IR spectra and measured translational SDC of the native and cross-linked αB-crystallins. Fig. (2) presents IR spectra of the Amide I peak that is very sensitive to the protein secondary structure composition. It is seen that native and cross-linked proteins reveal no secondary structure differences. Hence, the structural effect on the chaperone-like activity can be ruled out.

Bottom Line: The comparison of the chaperone-like activity of native and covalently cross-linked human alphaB-crystallins has confirmed the important role of the subunit mobility in the chaperoning mechanism.Our data clearly demonstrate that the chaperone-like activity of alpha-crystallin is not only a surface phenomenon as was suggested by some researchers.

View Article: PubMed Central - PubMed

Affiliation: Kazan Institute of Biochemistry and Biophysics, Russian Academy of Sciences, Kazan, Russia.

ABSTRACT
The comparison of the chaperone-like activity of native and covalently cross-linked human alphaB-crystallins has confirmed the important role of the subunit mobility in the chaperoning mechanism. Our data clearly demonstrate that the chaperone-like activity of alpha-crystallin is not only a surface phenomenon as was suggested by some researchers.

No MeSH data available.