❞ كتاب Chaperonin Protocols ❝ ⏤ Christine Schneider

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نبذه عن الكتاب:

Purification of Archaeal Chaperonin
from Sulfolobus shibatae
Elsie Quaite-Randall and Andrzej Joachimiak
1. Introduction
Sulfolobus shibatae is a hyperthermophilic archaeon that was first identified
living in acidic geothermal hot springs. This organism grows optimally at pH
3.0–4.0 and 83°C (1), however it grows over the temperature range of 75–
85°C. When S. shibatae is subjected to higher temperatures (85–90°C) a heatshock response is observed and the major protein induced is a large ring
structure TF55 (2), also called archaeosome (3) or rosettasome (4), which is
composed of two different subunits (4), designated _ and ` (3,4). Apart from
the presence of two subunits, another difference between this molecule and the
prokaryotic GroEL is the number of subunits per ring. In S. shibatae, nine
subunits form each ring compared with seven in GroEL.
The similarity of this double ring (2,3) to that of GroEL, together with the
fact that the subunits were 60 kDa, it was a heat-shock protein, and it was
active in protein folding, suggested that it was the archaeal chaperonin (2) and
was similar in function to GroEL. However, comparison of the primary structure showed that both subunits were more closely related to the TCP-1 family
of polypeptides, the eukaryotic cytosolic chaperonin (2,4,5). In contrast to the
archaeal chaperonin, the eukaryotic cytosolic chaperonin comprises eight
sequence-related polypeptides, which also form the characteristic “double
doughnut.” The archaeal chaperonin therefore gives us a simplified version of
the eukaryotic chaperonin by which it may be possible to determine characteristics of the eukaryotic chaperonin. Archaeal and mammalian cytoplasmic
chaperonins are often referred to as Type II chaperonins. The chaperonin from
S. shibatae is a Type II chaperonin (6) and is related, by primary sequence

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