Effect of crowding and chaperones on self-association, aggregation and reconstitution of apophosphorylase b

被引：17

作者：

Chebotareva, Natalia A. ^{[1
]}

Eronina, Tatyana B. ^{[1
]}

Roman, Svetlana G. ^{[1
]}

Poliansky, Nikolay B. ^{[2
]}

Muranov, Konstantin O. ^{[2
]}

Kurganov, Boris I. ^{[1
]}

机构：

[1] Russian Acad Sci, Bach Inst Biochem, Moscow 119071, Russia

[2] Russian Acad Sci, Emanuel Inst Biochem Phys, Moscow 119991, Russia

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2013年 / 60卷

基金：

俄罗斯基础研究基金会;

关键词：

Muscle glycogen phosphorylase b; Reconstruction of holoenzyme; Self-association; Aggregation; Crowding; RABBIT SKELETAL-MUSCLE; HEAT-SHOCK-PROTEIN; GLYCOGEN-PHOSPHORYLASE-B; ALPHA-CRYSTALLIN; PYRIDOXAL; 5-PHOSPHATE; SUBUNIT EXCHANGE; MOLECULAR CHAPERONE; THERMAL AGGREGATION; MECHANISM; PROLINE;

D O I：

10.1016/j.ijbiomac.2013.05.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

It was shown that the rate of reconstruction of muscle glycogen phosphorylase b (Phb) from apoenzyme and pyridoxal 5'-phosphate decreased under crowding conditions. The effect of crowding was counteracted by chaperones (alpha-crystallin and proline). Sedimentation analysis shows that crowding stimulates the formation of high-molecular-weight associates at 25 degrees C, whereas chaperones stabilize small oligomers. The study of the kinetics of apoPhb aggregation at 37 degrees C showed that the anti-aggregation activity of chaperones decreased under crowding conditions. When studying the sedimentation behavior of the mixture of apoPhb and alpha-crystallin, the complexes between unfolded apoPhb and dissociated forms of alpha-crystallin were observed. It is assumed that these complexes are responsible for realization of the chaperone-like activity of alpha-crystallin under crowding conditions. (c) 2013 Elsevier B.V. All rights reserved.

引用

页码：69 / 76

页数：8

共 62 条

[1] αB-Crystallin Polydispersity Is a Consequence of Unbiased Quaternary Dynamics [J].

Baldwin, Andrew J. ;

Lioe, Hadi ;

Robinson, Carol V. ;

Kay, Lewis E. ;

Benesch, Justin L. P. .

JOURNAL OF MOLECULAR BIOLOGY, 2011, 413 (02) :297-309

[2] Natural Osmolytes Remodel the Aggregation Pathway of Mutant Huntingtin Exon 1 [J].

Borwankar, Tejas ;

Roethlein, Christoph ;

Zhang, Gong ;

Techen, Anne ;

Dosche, Carsten ;

Ignatova, Zoya .

BIOCHEMISTRY, 2011, 50 (12) :2048-2060

[3] Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation [J].

Brown, Patrick H. ;

Schuck, Peter .

BIOPHYSICAL JOURNAL, 2006, 90 (12) :4651-4661

[4] ALPHA-CRYSTALLIN - MOLECULAR CHAPERONE AND PROTEIN SURFACTANT [J].

CARVER, JA ;

AQUILINA, JA ;

COOPER, PG ;

WILLIAMS, GA ;

TRUSCOTT, RJW .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1994, 1204 (02) :195-206

[5] The chemical chaperone proline relieves the thermosensitivity of a dnaK deletion mutant at 42°C [J].

Chattopadhyay, MK ;

Kern, R ;

Mistou, MY ;

Dandekar, AM ;

Uratsu, SL ;

Richarme, G .

JOURNAL OF BACTERIOLOGY, 2004, 186 (23) :8149-8152

[6] Effect of molecular crowding on the enzymes of glycogenolysis [J].

Chebotareva, N. A. .

BIOCHEMISTRY-MOSCOW, 2007, 72 (13) :1478-1490

[7] Role of thermoinduced dissociation in interaction between α-crystallin as an oligomeric chaperone and glyceraldehyde-3-phosphate dehydrogenase as an oligomeric protein substrate [J].

Chebotareva, N. A. ;

Kurganov, B. I. ;

Muranov, K. O. ;

Asryants, R. A. ;

Ostrovsky, M. A. .

DOKLADY BIOCHEMISTRY AND BIOPHYSICS, 2009, 428 (01) :245-248

[8]

Chebotareva N A, 1995, Biokhimiia, V60, P2030

[9] Biochemical effects of molecular crowding [J].

Chebotareva, NA ;

Kurganov, BI ;

Livanova, NB .

BIOCHEMISTRY-MOSCOW, 2004, 69 (11) :1239-+

[10]

Chebotareva NA, 2002, PROG COLL POL SCI S, V119, P70

← 1 2 3 4 5 6 7 →