Small heat shock proteins: molecular structure and chaperone function

Sun, Yu; MacRae, Thomas H.

doi:10.1007/s00018-005-5190-4

Cited by 437 publications

(374 citation statements)

References 163 publications

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“…According to Vicart et al (1998), their high expression level would allow them to exert an intermediate protective effect in response to stress conditions with no lag time necessary for protein synthesis. They constitute a dynamic complex (Sun and MacRae, 2005). This complex is implicated in the control of phosphorylation of myosin light chains, control of translation via the factor eIF4G, regulation of the apoptotic pathway by sequestration of Bcl-X and Bax, protection against aggregation of actin, desmin, titin and myosin and finally protection against heat shock of the citrate synthase and the malate dehydrogenase enzymes of the oxidative metabolism.…”

Section: Hspsmentioning

confidence: 99%

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Guillemin

Jurie

Cassar-Malek

et al. 2011

Animal

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Some proteins have been revealed as biomarkers for beef tenderness by previous studies. These markers could be used in immunological tests to predict beef tenderness, in living animals as well as in carcasses. It is well known that rearing practices modify the amounts of mRNA and proteins. Therefore, the reliability of protein tests could be affected by livestock and biological effects such as production systems, breed, muscle and animal type. This study analysed the effects of animal and muscle type on 24 proteins. The animals studied were 67 young bulls and 44 steers of the Charolais breed, and muscles were Longissimus thoracis and Semitendinosus. Protein amounts were determined by Dot blot, an immunological technique. Results showed that expressions of 20 proteins were influenced by animal and/or muscle type. These results could lead to modifications and adaptations of prediction tests according to rearing practice, bovine breed and beef cut.

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Section: Hspsmentioning

confidence: 99%

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Guillemin

Jurie

Cassar-Malek

et al. 2011

Animal

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“…These residues bind to hydrophobic patches on other proteins and are central to the formation of oligomers as well as sHSP-substrate complexes. As a consequence, truncations of the N-terminal arm affect both the oligomer assembly and chaperone activity of many sHSPs (Studer et al 2002;Sun and MacRae 2005). A study of the sHSP AgsA from Salmonella enterica demonstrated that truncations of different lengths at its termini resulted in drastic differences in the oligomeric state, which ranged from dimers to 22-mers.…”

Section: Introductionmentioning

confidence: 99%

Characterization of rice small heat shock proteins targeted to different cellular organelles

Mani

Ramakrishna

Suguna

2015

Cell Stress and Chaperones

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Small heat shock proteins (sHSPs) are a family of ATP-independent molecular chaperones which prevent cellular protein aggregation by binding to misfolded proteins. sHSPs form large oligomers that undergo drastic rearrangement/dissociation in order to execute their chaperone activity in protecting substrates from stress. Substrate-binding sites on sHSPs have been predominantly mapped on their intrinsically disordered N-terminal arms. This region is highly variable in sequence and length across species, and has been implicated in both oligomer formation and in mediating chaperone activity. Here, we present our results on the functional and structural characterization of five sHSPs in rice, each differing in their subcellular localisation, viz., cytoplasm, nucleus, chloroplast, mitochondria and peroxisome. We performed activity assays and dynamic light scattering studies to highlight differences in the chaperone activity and quaternary assembly of sHSPs targeted to various organelles. By cloning constructs that differ in the length and sequence of the tag in the N-terminal region, we have probed the sensitivity of sHSP oligomer assembly and chaperone activity to the length and amino acid composition of the N-terminus. In particular, we have shown that the incorporation of an N-terminal tag has significant consequences on sHSP quaternary structure.

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“…Small HSPs (sHSPs) comprise the most widespread but also the most poorly conserved family of molecular chaperones. sHSPs share characteristic features, including a conserved -crystallin domain, formation of large oligomers, induction by stress conditions and chaperone activity (Haslbeck et al, 2005;Sun and MacRae, 2005). It is generally accepted that HSPs protect organisms from the detrimental effects of heat and possibly other stressors, including various chemicals, heavy metals, cold, oxidative stress, osmotic stress and desiccation (Kregel, 2002;Lindquist, 1986;Somero, 1995).…”

Section: Introductionmentioning

confidence: 99%

Natural annual cycle of heat shock protein expression in land snails: desertversusMediterranean species ofSphincterochila

Arad

Mizrahi

Goldenberg

et al. 2010

Journal of Experimental Biology

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SUMMARYLand snails are subject to daily and seasonal variations in temperature and in water availability, and have evolved annual cycles of activity and aestivation as part of their survival strategy. We tested in the field whether adaptation to different habitats affects the endogenous levels of heat shock proteins (HSPs) in two closely related Sphincterochila snail species, a desiccation-resistant desert species, Sphincterochila zonata, and a Mediterranean-type, desiccation-sensitive species, S. cariosa. We examined HSP levels in various tissues of snails during aestivation and after resumption of activity. Our study shows that, during aestivation, S. cariosa had higher standing stocks of Hsp70 in the foot and the hepatopancreas, and of small HSPs (sHSPs) in all the examined tissues, whereas S. zonata had higher stocks of Hsp70 in the kidney and of Hsp90 in the kidney and in the hepatopancreas. Arousal induced a general upregulation of HSPs, except for Hsp90, the expression of which in the foot was higher during aestivation. We suggest that the stress protein machinery is upregulated during arousal in anticipation of possible oxidative stress ensuing from the accelerating metabolic rate and the exit from the deep hypometabolic state. Our findings support the concept that, in land snails, aestivation and activity represent two distinct physiological states, and suggest that land snails use HSPs as important components of the aestivation mechanism, and as part of their survival strategy during and after arousal. Our study also indicates that adaptation to different habitats results in the development of distinct strategies of HSP expression with likely consequences for the ecology and distribution of land snails. Supplementary material available online at

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Small heat shock proteins: molecular structure and chaperone function

Cited by 437 publications

References 163 publications

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Characterization of rice small heat shock proteins targeted to different cellular organelles

Natural annual cycle of heat shock protein expression in land snails: desertversusMediterranean species ofSphincterochila

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