HSPD1
HSPD1 (heat shock protein family D (Hsp60) member 1, also known as HSP60, GroEL or SPG13) encodes a mitochondrial chaperonin of the HSP60 family. It supports protein import and the folding and assembly of proteins in the mitochondrial matrix. Browse Assay Genie's current range of HSPD1 research reagents below, or read on for the biology behind the target.
HSPD1 is a chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, it facilitates the correct folding of imported proteins, and it may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional unit is a back-to-back double ring, each ring made up of seven Hsp60 subunits.
The folding mechanism is a cyclic reaction. Each Hsp60 ring binds one unfolded substrate protein, then binds ATP and associates with a heptameric ring of the co-chaperonin Hsp10. The substrate is sequestered in the inner cavity of Hsp60, where for a period of time it can fold undisturbed by other cell components. Synchronous ATP hydrolysis in all Hsp60 subunits then dissociates the rings and releases ADP and the folded substrate. The protein belongs to the chaperonin (HSP60) family and is localised to the mitochondrial matrix. HGNC places it in the chaperonins and the mitochondrial nucleoid associated proteins gene groups.
The HSPD1 gene sits next to a related family member, and the region between the two genes works as a bidirectional promoter. Several pseudogenes are associated with the gene, and two transcript variants encode the same protein. NCBI Gene notes that the protein may also act as a signalling molecule in the innate immune system. Mutations in the gene cause autosomal recessive spastic paraplegia 13, which accounts for the SPG13 alias. Earlier names include heat shock 60kD protein 1 (chaperonin), and the bacterial GroEL name reflects the family relationship. Mouse and rat each carry an ortholog named Hspd1.
HSPD1 assists the folding of imported proteins and the refolding of polypeptides unfolded under stress in the matrix, making it a central subject for studies of mitochondrial protein quality.
The ATP-driven cycle of Hsp60 double rings and Hsp10 co-chaperonin rings provides a model system for how substrates fold within a sequestered cavity.
Mutations in HSPD1 cause autosomal recessive spastic paraplegia 13, linking the chaperonin to research on inherited neurological disorders.
NCBI Gene reports that the mitochondrial HSPD1 protein may function as a signalling molecule in the innate immune system, opening questions beyond folding.
HSPD1 is a mitochondrial chaperonin that, together with Hsp10, helps imported proteins fold correctly in the matrix. Hsp60 rings enclose an unfolded substrate, and ATP binding and hydrolysis drive folding and release. It may also help refold polypeptides unfolded under stress.
HSPD1 is also called HSP60, GroEL and SPG13. Earlier names include heat shock 60kD protein 1 (chaperonin) and spastic paraplegia 13 (autosomal dominant). UniProt lists the protein as 60 kDa heat shock protein, mitochondrial. NCBI Gene notes two transcript variants that encode the same protein.
Mutations in HSPD1 cause autosomal recessive spastic paraplegia 13. The gene has orthologs named Hspd1 in mouse and rat, and the protein belongs to the broader chaperonin family. Check the datasheet of any product for its validated reactivity.
Other chaperones, co-chaperonins and mitochondrial proteostasis targets that complement HSPD1 research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P10809; product specifications from Assay Genie datasheets.