Divergence of the mRNA targets for the Ssb proteins of bacteriophages T4 and RB69.docVIP

Virology Journal BioMedCentral Research Open Access Divergence of the mRNA targets for the Ssb proteins of bacteriophages T4 and RB69 Jamilah M Borjac-Natour1,2, Vasiliy M Petrov1 and Jim D Karam*1 Address: 1Department of Biochemistry SL 43, Tulane University Health Sciences Center, 1430 Tulane Avenue, New Orleans, LA 70112, USA and 2Lebanese American University, PO Box 13-5053, Mailbox S-37, Beirut, Lebanon Email: Jamilah M Borjac-Natour - jamilahborjac@; Vasiliy M Petrov - vpetrov@; Jim D Karam* - karamoff@ * Corresponding author Published: 17 September 2004 Received: 12 July 2004 Accepted: 17 September 2004 Virology Journal 2004, 1:4 doi:10.1186/1743-422X-1-4 This article is available from: /content/1/1/4 ? 2004 Borjac-Natour et al; licensee BioMed Central Ltd. This is an open-access article distributed under the terms of the Creative Commons Attribution License (/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Ssb protein, gp32, RNA-binding proteins, DNA-binding proteinstranslational control, DNA replication Abstract The single-strand binding (Ssb) protein of phage T4 (T4 gp32, product of gene 32) is a mRNA- specific autogenous translational repressor, in addition to being a sequence-independent ssDNA- binding protein that participates in phage DNA replication, repair and recombination. It is not clear how this physiologically essential protein distinguishes between specific RNA and nonspecific nucleic acid targets. Here, we present phylogenetic evidence suggesting that ssDNA and specific RNA bind the same gp32 domain and that plasticity of this domain underlies its ability to configure certain RNA structures for specific binding. We have cloned and characterized gene 32 of phage RB69, a relative of T4 We observed that RB69 gp32 and T4 gp32 have nearly identical ssDNA binding domains, but diverge in their C-