The Bacterial Cytoskeleton based on Bacterial Translation Elongation Factor EF-Tu: Novel Insights

Frank Mayer

doi:10.31579/2690-1919/224

Abstract

Bacteria possess an EF-Tu-based cytoskeleton.This article presents a short review. A number of questions which are not discussed in the former publications can be asked, such as: all bacteria possess a ribosomal protein synthesis system and, hence, also EF-Tu. EF-Tu is produced in an amount that is higher than the need for a function as translation elogation factor in ribsomal protein synthesis. This article tries to answer the question regarding the surplus of EF-Tu: formation of a "cell-wide web" by self-assembly as a feafure that stabilizes cell integrity. An additional question can be asked: what is the origin of this bacterial cytoskeleton? This article contains a speculation on this topic. A third question regards the'ntteructjon of ribosomes in the process of protemsynthesis: does the EF-Tu protein move to the ribosome, or does the ribosome move to the EF-Tu intergated in a fibril of the bacterial cytoskeleton? The former publication depicts electron micrographs which show colocalizatton of botth entities. EF-Tu is an example for aprotein with two independent functions: participation in the ribosomal protein synthesis as a kanslation elongation factor, and component of a bacterial cytoskeleton. This situation can open up a discussion ofthe sequence of events and states of early cells during evolution.

Highlights

Introduction and Mini ReviewIn former publications [1,2,3,4,5,6] and (Figure 1), the structural organization of the EF-Tu-based bacterial cytoskeleton is described
The elongation factor EF-Tu is known for its important role in the bacterial ribosomal protein synthesis
In a former publication [10] it was stated that Ef-Tu in bacterial cells is produced in much higher numbers as compared to the need of its role in protein synthesis

Summary

Introduction

Introduction and Mini ReviewIn former publications [1,2,3,4,5,6] and (Figure 1), the structural organization of the EF-Tu-based bacterial cytoskeleton is described. No explanations were offered for the reason of this fact In this former publication it was reported that EF-Tu can form fibrils consisting of many EF-Tu molecules bound to each other by non-covalent binding. The idea that bacteria contain a cytoskeleton did come up by a surprising phenomenon: bacteria did maintain their typical shape and size even after removal of all layers of the cell wall and of its cytoplasmic membrane [11] At this time publications such as [8] did report that bacteria possess a cytoskeleton consisting of proteins related to actin. The exact amino acid sequences of these sites are known [12] This interpretation was supported by electron microscopic images obtained during investigations of fibrils isolated from artificially lysed bacteria, and of fibrils created, by polymerization, using isolated EF-Tu proteins (Figure 2)

Discussion

Conclusion