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Roles of Hsp70s in Stress Responses of Microorganisms, Plants, and Animals.

Yu A, Li P, Tang T, Wang J, Chen Y, Liu L - Biomed Res Int (2015)

Bottom Line: Most research on Hsp70s has focused on the mechanisms of their functions as molecular chaperones, but recently, studies on stress responses are coming to the forefront.Moreover, functions of human Hsp70s are related to diseases including neurological disorders, cancer, and virus infection.In this review, we provide an overview of the specific roles of Hsp70s in response to stress, particularly abiotic stress, in all living organisms.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Economic Plants and Biotechnology, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming, Yunnan 650201, China ; Yunnan Key Laboratory for Wild Plant Resources, Kunming, Yunnan 650201, China.

ABSTRACT
Hsp70s (heat shock protein 70s) are a class of molecular chaperones that are highly conserved and ubiquitous in organisms ranging from microorganisms to plants and humans. Most research on Hsp70s has focused on the mechanisms of their functions as molecular chaperones, but recently, studies on stress responses are coming to the forefront. Hsp70s play key roles in cellular development and protecting living organisms from environmental stresses such as heat, drought, salinity, acidity, and cold. Moreover, functions of human Hsp70s are related to diseases including neurological disorders, cancer, and virus infection. In this review, we provide an overview of the specific roles of Hsp70s in response to stress, particularly abiotic stress, in all living organisms.

No MeSH data available.


Related in: MedlinePlus

Analysis of the conserved domains of partial Hsp70s in cytoplasm group from various kingdoms. The Hsp70 members from Saccharomyces cerevisiae (Sc), Homo sapiens (Hs), Drosophila melanogaster (Dm), Chlamydomonas reinhardtii (Cre), Physcomitrella patens (Pp), Selaginella moellendorffii (Sm), Oryza sativa (Os), Arabidopsis thaliana (At), and Populus trichocarpa (Pt).
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fig1: Analysis of the conserved domains of partial Hsp70s in cytoplasm group from various kingdoms. The Hsp70 members from Saccharomyces cerevisiae (Sc), Homo sapiens (Hs), Drosophila melanogaster (Dm), Chlamydomonas reinhardtii (Cre), Physcomitrella patens (Pp), Selaginella moellendorffii (Sm), Oryza sativa (Os), Arabidopsis thaliana (At), and Populus trichocarpa (Pt).

Mentions: Hsps are pivotal molecular chaperones that function in response to proteotoxic stress by refolding misfolded proteins. Hsp70 (called DnaK in prokaryotes) is a 70-kDa protein that represents the best-known heat shock protein [4]. Hsp70s are highly conserved and exist in all organisms ranging from microorganisms to plants and humans. Structurally, Hsp70s contain a nucleotide-binding domain (NBD), acting as a ATPase domain, a substrate-binding domain (SBD), and a C-terminal lid region that covers the SBD. Usually, the NBD is around 45 kDa and the SBD is around 15 kDa. By contrast, the length or sequence of the C-terminal region varies and in some cases contains organelle-specific retention motifs [5]. The NBD and SBD are highly conserved, while the C-terminal region has varied to some extent (Figure 1).


Roles of Hsp70s in Stress Responses of Microorganisms, Plants, and Animals.

Yu A, Li P, Tang T, Wang J, Chen Y, Liu L - Biomed Res Int (2015)

Analysis of the conserved domains of partial Hsp70s in cytoplasm group from various kingdoms. The Hsp70 members from Saccharomyces cerevisiae (Sc), Homo sapiens (Hs), Drosophila melanogaster (Dm), Chlamydomonas reinhardtii (Cre), Physcomitrella patens (Pp), Selaginella moellendorffii (Sm), Oryza sativa (Os), Arabidopsis thaliana (At), and Populus trichocarpa (Pt).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4663327&req=5

fig1: Analysis of the conserved domains of partial Hsp70s in cytoplasm group from various kingdoms. The Hsp70 members from Saccharomyces cerevisiae (Sc), Homo sapiens (Hs), Drosophila melanogaster (Dm), Chlamydomonas reinhardtii (Cre), Physcomitrella patens (Pp), Selaginella moellendorffii (Sm), Oryza sativa (Os), Arabidopsis thaliana (At), and Populus trichocarpa (Pt).
Mentions: Hsps are pivotal molecular chaperones that function in response to proteotoxic stress by refolding misfolded proteins. Hsp70 (called DnaK in prokaryotes) is a 70-kDa protein that represents the best-known heat shock protein [4]. Hsp70s are highly conserved and exist in all organisms ranging from microorganisms to plants and humans. Structurally, Hsp70s contain a nucleotide-binding domain (NBD), acting as a ATPase domain, a substrate-binding domain (SBD), and a C-terminal lid region that covers the SBD. Usually, the NBD is around 45 kDa and the SBD is around 15 kDa. By contrast, the length or sequence of the C-terminal region varies and in some cases contains organelle-specific retention motifs [5]. The NBD and SBD are highly conserved, while the C-terminal region has varied to some extent (Figure 1).

Bottom Line: Most research on Hsp70s has focused on the mechanisms of their functions as molecular chaperones, but recently, studies on stress responses are coming to the forefront.Moreover, functions of human Hsp70s are related to diseases including neurological disorders, cancer, and virus infection.In this review, we provide an overview of the specific roles of Hsp70s in response to stress, particularly abiotic stress, in all living organisms.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory of Economic Plants and Biotechnology, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming, Yunnan 650201, China ; Yunnan Key Laboratory for Wild Plant Resources, Kunming, Yunnan 650201, China.

ABSTRACT
Hsp70s (heat shock protein 70s) are a class of molecular chaperones that are highly conserved and ubiquitous in organisms ranging from microorganisms to plants and humans. Most research on Hsp70s has focused on the mechanisms of their functions as molecular chaperones, but recently, studies on stress responses are coming to the forefront. Hsp70s play key roles in cellular development and protecting living organisms from environmental stresses such as heat, drought, salinity, acidity, and cold. Moreover, functions of human Hsp70s are related to diseases including neurological disorders, cancer, and virus infection. In this review, we provide an overview of the specific roles of Hsp70s in response to stress, particularly abiotic stress, in all living organisms.

No MeSH data available.


Related in: MedlinePlus