The role of ribosomal proteins L7 and L-12 in polypeptide chain initiation in Escherichia coli.

نویسندگان

  • A H Lockwood
  • U Maitra
  • N Brot
  • H Weissbach
چکیده

Proteins L, and LIZ from the 50 S ribosomal subunit are required for polypeptide chain initiation in Escherchia coli. Ribosomes deficient in these proteins cannot participate in initiation factor IF-2 dependent hydrolysis of guanosine triphosphate (either “coupled” or “uncoupled” from initiation); activity can be restored by the addition of either L? or LlZ. N-Formyl methionyl transfer RNA binding to ribosomes is also impaired in the absence of L7 and LIZ. The results indicate that L7 or LIZ is required for the catalytic function of IF-Z in binding N-formyl methionyl transfer RNA to ribosomes. In each reaction tested, L7 and LIZ are about equal in efficiency in restoring activity to depleted 50 S subunits. These results are discussed in light of the current information on the role of these ribosomal proteins in other partial reactions or protein synthesis.

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

High Level Expression of Recombinant Ribosomal Protein (L7/L12) from Brucella abortus and Its Reaction with Infected Human Sera

Brucellosis, caused by Brucella spp., is an important zoonotic disease that causes abortion and infertility in cattle and undulant fever in humans. Various studies have examined cell-free native and recombinant proteins as candidate protective antigens in animal models. Among Brucella immunogenes, antigen based on ribosomal preparation has been widely investigated. In this study, the immunogeni...

متن کامل

Enterotoxigenic Escherichia coli infection induces tight junction proteins expression in mice

Enterotoxigenic Escherichia coli (ETEC) causes diarrhea in travelers, young children and piglets, but the precise pathogenesis of ETEC induced diarrhea is not fully known. Recent investigations have shown that tight junction (TJ) proteins and aquaporin 3 (AQP 3) are contributing factors in bacterial diarrhea. In this study, using immunoblotting and immunohistochemistry analyses, we found that E...

متن کامل

Escherichia coli ribosomal protein L10 is rapidly degraded when synthesized in excess of ribosomal protein L7/L12.

In Escherichia coli the genes encoding ribosomal proteins L10 and L7/12, rplJ and rplL, respectively, are cotranscribed and subject to translational coupling. Synthesis of both proteins is coordinately regulated at the translational level by binding of L10 or a complex of L10 and L7/L12 to a single target in the mRNA leader region upstream of rplJ. Unexpectedly, small deletions that inactivated...

متن کامل

Temperature-dependent variation in the extent of methylation of ribosomal proteins L7 and L12 in Escherichia coli.

The amount of epsilon-N-monomethyllysine in ribosomal proteins L7 and L12 in Escherichia coli is dependent upon the cell growth temperature. At 37 degrees C or above, very small amounts were detected. Dramatic increase in the content of epsilon-N-monomethyllysine in these proteins was observed when the growth temperature was lowered.

متن کامل

The RNA binding properties of "native" protein-protein complexes isolated from the Escherichia coli ribosome.

The assembly of the Escherichia coli ribosome is based on many specific interactions between the ribosomal components. Direct evidence for single proteinRNA interactions has been well established (reviewed in ref. [l] ). Various observations provide circumstantial support for the existence of protein-protein complexes in the ribosome. For example, cooperative protein binding effects have been o...

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:
  • The Journal of biological chemistry

دوره 249 4  شماره 

صفحات  -

تاریخ انتشار 1974