Polyribosomes Are Molecular 3D Nanoprinters That Orchestrate the Assembly of Vault Particles

نویسندگان

  • Jan Mrazek
  • Daniel Toso
  • Sergey Ryazantsev
  • Xing Zhang
  • Z. Hong Zhou
  • Beatriz Campo Fernandez
  • Valerie A. Kickhoefer
  • Leonard H. Rome
چکیده

Ribosomes are molecular machines that function in polyribosome complexes to translate genetic information, guide the synthesis of polypeptides, and modulate the folding of nascent proteins. Here, we report a surprising function for polyribosomes as a result of a systematic examination of the assembly of a large ribonucleoprotein complex, the vault particle. Structural and functional evidence points to a model of vault assembly whereby the polyribosome acts like a 3D nanoprinter to direct the ordered translation and assembly of the multi-subunit vault homopolymer, a process which we refer to as polyribosome templating. Structure-based mutagenesis and cell-free in vitro expression studies further demonstrated the critical importance of the polyribosome in vault assembly. Polyribosome templating prevents chaos by ensuring efficiency and order in the production of large homopolymeric protein structures in the crowded cellular environment and might explain the origin of many polyribosome-associated molecular assemblies inside the cell.

برای دانلود 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

Reovirus-specific messenger ribonucleoprotein particles from HeLa cells.

When reovirus-infected Hela cells are incubated at 43 degrees C virus-specific messenger RNA is released from the polysomes. It accumulates free in the cytoplasm as messenger ribonucleoprotein particles (mRNPs). These particles have a sedimentation rate of about 50S and a buoyant density in CsCL of 1.42 g/cm3. Reovirus mRNPs contain, besides all three size classes of reovirus messenger RNA, the...

متن کامل

The vault exterior shell is a dynamic structure that allows incorporation of vault-associated proteins into its interior.

Vaults are 13 million Da ribonucleoprotein particles with a highly conserved structure. Expression and assembly by multimerization of an estimated 96 copies of a single protein, termed the major vault protein (MVP), is sufficient to form the minimal structure and entire exterior shell of the barrel-shaped vault particle. Multiple copies of two additional proteins, VPARP and TEP1, and a small un...

متن کامل

The Mr 193,000 vault protein is up-regulated in multidrug-resistant cancer cell lines.

Vaults are 13 megadalton ribonucleoprotein particles composed largely of the major vault protein (MVP) and two high molecular weight proteins, p240 and p193, and a small vault RNA (vRNA). Increased levels of MVP expression, vault-associated vRNA, and vaults have been linked directly to multidrug resistance (MDR). To further define the putative role of vaults in MDR, we produced monoclonal antib...

متن کامل

Vault poly(ADP-ribose) polymerase is associated with mammalian telomerase and is dispensable for telomerase function and vault structure in vivo.

Vault poly(ADP-ribose) polymerase (VPARP) was originally identified as a minor protein component of the vault ribonucleoprotein particle, which may be involved in molecular assembly or subcellular transport. In addition to the association of VPARP with the cytoplasmic vault particle, subpopulations of VPARP localize to the nucleus and the mitotic spindle, indicating that VPARP may have other ce...

متن کامل

Synthesis and characterization of supramolecule self-assembly polyamidoamine (PAMAM) G1-G1 NH2, CO2H end group Megamer

Supramolecule self assembly polyamidoamine (PAMAM) dendrimer refers to the chemical systems made up of a discrete number of assembled molecular subunits or components. These strategies involve the covalent assembly of hierarchical components reactive monomers, branch cells or dendrons around atomic or molecular cores according to divergent/convergent dendritic branching principles, systematic f...

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

برای دانلود 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

عنوان ژورنال:

دوره 8  شماره 

صفحات  -

تاریخ انتشار 2014