TIM-14 Protein, S.cerevisiae

The TIM-14 protein is an important component of the PAM complex and is required for the transport of transit peptide-containing proteins from the inner membrane to the mitochondrial matrix using ATP. TIM-14 Protein, S.cerevisiae is the recombinant TIM-14 protein, expressed by E. coli , with tag free. The total length of TIM-14 Protein, S.cerevisiae is 70 a.a., with molecular weight of ~9.0 kDa.

TIM-14 stands as an indispensable constituent of the PAM complex, a pivotal assembly instrumental in the ATP-dependent translocation of transit peptide-containing proteins from the inner mitochondrial membrane into the mitochondrial matrix. Within this intricate molecular machinery, TIM-14 assumes a critical role in stimulating the activity of mtHSP70 (SSC1). It engages in a dynamic existence, forming homodimers and heterodimers with PAM16/TIM16. While homodimerization might not hold significance in vivo, the formation of heterodimers proves to be essential for the nuanced regulation of mtHSP70 activity. As an integral part of the larger PAM complex, TIM-14 collaborates seamlessly with mtHsp70, MGE1, TIM44, PAM16, PAM17, and PAM18/TIM14, collectively contributing to the orchestration of mitochondrial protein translocation. Additionally, TIM-14 establishes direct interactions with mtHsp70, reinforcing its role in the intricate network of molecular associations involved in ensuring the efficiency and precision of mitochondrial protein translocation. Furthermore, its direct interaction with the TIM17 subunit of the TIM23 complex adds another layer of complexity to its involvement in mitochondrial protein transport processes.

Others

E. coli

Tag Free

Q07914 (F99-K168)

850694  [NCBI]

FLKGGFDPKMNSKEALQILNLTENTLTKKKLKEVHRKIMLANHPDKGGSPFLATKINEAKDFLEKRGISK

Approximately 9.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.