Reconstitution of peptide bond formation with Escherichia coli 23S ribosomal RNA domains.

نویسندگان

  • I Nitta
  • Y Kamada
  • H Noda
  • T Ueda
  • K Watanabe
چکیده

It was recently demonstrated that peptide bond formation can occur using an Escherichia coli naked 23S ribosomal RNA without any of the ribosomal proteins. Here, the six domains of the 23S ribosomal RNA were individually synthesized and shown to be capable, when complexed together, of stimulating the reaction. Omission and addition experiments indicated that the activity could be reconstituted solely by domain V at a concentration 10 times higher than that of the intact 23S ribosomal RNA, whereas domain VI could enhance the activity in trans. These findings suggest that fragments of an RNA molecule have the ability to associate into a functional whole.

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

Possible involvement of Escherichia coli 23S ribosomal RNA in peptide bond formation.

Experimental results are presented suggesting that 23S rRNA is directly involved in the peptide bond formation usually performed on the ribosome. Although several reports have indicated that the eubacterial peptidyltransferase reaction does not necessarily require all the ribosomal proteins, the reconstitution of peptidyltransferase activity by a naked 23S rRNA without the help of any of the ri...

متن کامل

The A2453-C2499 wobble base pair in Escherichia coli 23S ribosomal RNA is responsible for pH sensitivity of the peptidyltransferase active site conformation.

Peptide bond formation, catalyzed by the ribosomal peptidyltransferase, has long been known to be sensitive to monovalent cation concentrations and pH. More recently, we and others have shown that residue A2451 in the peptidyltransferase center of the Escherichia coli 50S ribosomal subunit changes conformation in response to alterations in pH, depending on ionic conditions and temperature. Two ...

متن کامل

Cellular Morphology and Immunologic Properties of Escherichia coli Treated With Antimicrobial Antisense Peptide Nucleic Acid

  Background & Objectives: Antisense peptide nucleic acids (PNA) that target growth essential genes show potent bactericidal properties without cell lysis. We considered the possibility that whether PNA treatment influence the bacteria total nucleic acids content and apply approach to develop a new delivery system to Dendritic cells (DCs). DCs are the most potent antigen presenting cells in th...

متن کامل

The G2447A mutation does not affect ionization of a ribosomal group taking part in peptide bond formation.

Peptide bond formation on the ribosome is catalyzed by RNA. Kinetic studies using Escherichia coli ribosomes have shown that catalysis (>10(5)-fold overall acceleration) is due to a large part to substrate positioning. However, peptide bond formation is inhibited approximately 100-fold by protonation of a ribosomal group with pKa=7.5, indicating either a contribution of general acid-base cataly...

متن کامل

Kinetics and Thermodynamics of DbpA Protein’s C-Terminal Domain Interaction with RNA

DbpA is an Escherichia coli DEAD-box RNA helicase implicated in RNA structural isomerization in the peptide bond formation site. In addition to the RecA-like catalytic core conserved in all of the members of DEAD-box family, DbpA contains a structured C-terminal domain, which is responsible for anchoring DbpA to hairpin 92 of 23S ribosomal RNA during the ribosome assembly process. Here, surface...

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:
  • Science

دوره 281 5377  شماره 

صفحات  -

تاریخ انتشار 1998