Ribosomal Protein S1: An Important Trans-Translational Factor | OMICS International | Abstract
ISSN: 2168-9652

Biochemistry & Physiology: Open Access
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Research Article

Ribosomal Protein S1: An Important Trans-Translational Factor

Iwona K. Wower1, Nusrat Jahan2, Christian Zwieb3 and Jacek Wower1*
1Department of Animal Sciences, 210 Upchurch Hall, Auburn University, Auburn, AL 36849-5415, USA
2Department of Molecular Genetics and Microbiology, Life Sciences Building, Stony Brook University, Stony Brook, NY 11794-5222, USA
3University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78229, USA
*Corresponding Author : Jacek Wower
Department of Animal Sciences
210 Upchurch Hall, Auburn University
Auburn, AL 36849-5415, USA
Tel: +1 334 844 1508
Fax: +1 334 844 1519
E-mail: [email protected]
Received December 01, 2012; Accepted December 27, 2012; Published December 31, 2012
Citation: Wower IK, Jahan N, Zwieb C, Wower J (2013) Ribosomal Protein S1: An Important Trans-Translational Factor. Biochem Physiol S2:001. doi:10.4172/2168-9652.S2-001
Copyright: © 2013 Wower IK, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


S1 is an essential protein in Escherichia coli. Although not present in all bacteria, its importance for the initiation and elongation stages of protein synthesis is well established. Beside its roles as a ribosomal protein, S1 promotes transcriptional cycling, regulates bacteriophage T4 gene expression, forms a complex with the phage. λ protein β involved in recombination, and is a subunit of the fr and Qβ RNA bacteriophage replicases. Protein S1 was also shown to bind to tmRNA, an essential component of trans-translation. Although the physiological significance of protein S1 for trans-translation has been debated for many years, recent studies clearly demonstrate that protein S1 constitutes an important, yet poorly understood component of trans-translation. We show that binding of protein S1 to the free tmRNA is a prerequisite for the association between tmRNA and stalled ribosome. S1 transits the ribosome together with the tmRNA as defective proteins are targeted for proteolysis. These findings establish protein S1 as an important target for pharmacological intervention.