Go Back   Science Forums Biology Forum Molecular Biology Forum Physics Chemistry Forum > General Forum > Science News and Views
Register Search Today's Posts Mark Forums Read

Science News and Views The latest news and publications from Nature, Science, Cell and other journals. Post science topics and your thoughts here. Anything science related goes here.


[Protein Synthesis, Post-Translational Modification, and Degradation] Functional Interactions between the G' Subdomain of Bacterial Translation Factor EF-G and Ribosomal Protein L7/L12

[Protein Synthesis, Post-Translational Modification, and Degradation] Functional Interactions between the G' Subdomain of Bacterial Translation Factor EF-G and Ribosomal Protein L7/L12 - Science News and Views

[Protein Synthesis, Post-Translational Modification, and Degradation] Functional Interactions between the G' Subdomain of Bacterial Translation Factor EF-G and Ribosomal Protein L7/L12 - The latest news and publications from Nature, Science, Cell and other journals. Post science topics and your thoughts here. Anything science related goes here.


Reply
 
LinkBack Thread Tools Display Modes
  #1  
Old 12-14-2007, 02:47 PM
admin's Avatar
Administrator
 
Join Date: Nov 2005
Posts: 1,418
Thanks: 883
Thanked 68 Times in 58 Posts
Default [Protein Synthesis, Post-Translational Modification, and Degradation] Functional Interactions between the G' Subdomain of Bacterial Translation Factor EF-G and Ribosomal Protein L7/L12



[Protein Synthesis, Post-Translational Modification, and Degradation] Functional Interactions between the G' Subdomain of Bacterial Translation Factor EF-G and Ribosomal Protein L7/L12

Protein L7/L12 of the bacterial ribosome plays an important role in activating the GTP hydrolytic activity of elongation factor G (EF-G), which promotes ribosomal translocation during protein synthesis. Previously, we cross-linked L7/L12 from two residues (209 and 231) flanking -helix AG' in the G' subdomain of Escherichia coli EF-G. Here we report kinetic studies on the functional effects of mutating three neighboring glutamic acid residues (224, 228, and 231) to lysine, either singly or in combination. Two single mutations (E224K and E228K), both within helix AG', caused large defects in GTP hydrolysis and smaller defects in ribosomal translocation. Removal of L7/L12 from the ribosome strongly reduced the activities of wild type EF-G but had no effect on the activities of the E224K and E228K mutants. Together, these results provide evidence for functionally important interactions between helix AG' of EF-G and L7/L12 of the ribosome.
Reply With Quote
Reply

Tags
bacterial , degradation , efg , factor , functional , interactions , l7 or l12 , modification , posttranslational , protein , ribosomal , subdomain , synthesis , translation


Thread Tools
Display Modes

Posting Rules
You may not post new threads
You may not post replies
You may not post attachments
You may not edit your posts

BB code is On
Smilies are On
[IMG] code is On
HTML code is Off
Trackbacks are On
Pingbacks are On
Refbacks are On

Forum Jump


All times are GMT. The time now is 09:44 PM.


Powered by vBulletin® Version 3.8.4
Copyright ©2000 - 2014, Jelsoft Enterprises Ltd.
Copyright 2005 - 2012 Molecular Station | All Rights Reserved
Page generated in 0.10925 seconds with 15 queries