The ATP-driven protein translocation-motor of mitochondria

نویسندگان

  • Chitkala Satyanarayana
  • Martin Horst
چکیده

The majority of mitochondrial proteins are encoded in the nucleus. In the cytosol they are synthesized as precursor proteins which are transported into mitochondria. Protein import into mitochondria requires a concerted action of a variety of different proteins. For the transport of precursor proteins across the mitochondrial inner membrane and their folding in the matrix the mitochondrial hsp70 (mhsp70) chaperone plays an essential role. Mhsp70 is found in at least two protein complexes within mitochondria: together with Tim44 and mGrpE, mhsp70 forms the import-complex and together with Mdj1 and mGrpE i t forms a folding-complex. This review focuses on the function of the import-complex. It is believed that mhsp70 can act as a mechanochemical enzyme that actively pulls precursor proteins across the inner membrane.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Protein Translocation into the Intermembrane Space and Matrix of Mitochondria: Mechanisms and Driving Forces

Mitochondria contain two aqueous subcompartments, the matrix and the intermembrane space (IMS). The matrix is enclosed by both the inner and outer mitochondrial membranes, whilst the IMS is sandwiched between the two. Proteins of the matrix are synthesized in the cytosol as preproteins, which contain amino-terminal matrix targeting sequences that mediate their translocation through translocases...

متن کامل

Protein unfolding by mitochondria. The Hsp70 import motor.

Protein unfolding is a key step in the import of some proteins into mitochondria and chloroplasts and in the degradation of regulatory proteins by ATP-dependent proteases. In contrast to protein folding, the reverse process has remained largely uninvestigated until now. This review discusses recent discoveries on the mechanism of protein unfolding during translocation into mitochondria. The mit...

متن کامل

Stoichiometry of adenosine triphosphate-driven proton translocation in bovine heart submitochondrial particles.

Inward-directed proton translocation driven by ATP hydrolysis was investigated in bovine heart submitochondrial particles under conditions where no net pH change occurred upon ATP hydrolysis. A biphasic time course of ATP hydrolysis, due to the presence of adenylate kinase activity, was observed by following the release of 32Pi from [P,r32P]ATP under comparable conditions. An equation was deriv...

متن کامل

Protein unfolding by mitochondria

Protein unfolding is a key step in the import of some proteins into mitochondria and chloroplasts and in the degradation of regulatory proteins by ATP-dependent proteases. In contrast to protein folding, the reverse process has remained largely uninvestigated until now. This review discusses recent discoveries on the mechanism of protein unfolding during translocation into mitochondria. The mit...

متن کامل

A matrix ATP requirement for presequence translocation across the inner membrane of mitochondria.

The mitochondrial presequence initiates protein translocation across the inner membrane of mitochondria in a delta psi-dependent step. We have investigated the role of matrix ATP in this process. When matrix ATP was reduced to interfere with the function of mitochondrial heat shock protein 70, presequence translocation across the inner membrane was strongly inhibited. This was accompanied by th...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2001