RpoS protein is a σ factor of RNA polymerase that can control the expression of a group-specific gene, thus playing a vital role in bacteria. In bacteria, RpoS expression is under strict control and is mainly regulat...RpoS protein is a σ factor of RNA polymerase that can control the expression of a group-specific gene, thus playing a vital role in bacteria. In bacteria, RpoS expression is under strict control and is mainly regulated at three levels： transcription level, translation level and post-translational level. Environmental stress enters bacterial cells through signal transduction and leads to a series of variations in microenvironment, thereby causing changes of regulator and controlling its levels based on the direct and indirect interaction between regulator and RpoS protein. In addition, RpoS protein has played special roles in bacteria, therefore the changes of RpoS protein levels will lead to variations in expression levels of a large number of genes, thereby causing variations of bacterial response to different environmental stress and changes of certain characteristics of bacteria, which provides a new strategy for the control of bacterial diseases in the future. This paper reviewed the recent progress on the regulation of RpoS protein expression and its function in several common bacteria. Due to the functional complexity of RpoS protein, there are still a lot of unknown functions to be further identified.展开更多
[Objective] The study aimed to clone RPO30 gene from Sheeppox virus （SPPV） and predict the structure and function of the sequence. [Method] RPO30 gene of SPPV was cloned with PCR, linked into pMD18-T simple vector a...[Objective] The study aimed to clone RPO30 gene from Sheeppox virus （SPPV） and predict the structure and function of the sequence. [Method] RPO30 gene of SPPV was cloned with PCR, linked into pMD18-T simple vector and then transformed into E. coli DH5a. In blue-white screen, the white colonies were selected to prepare plasmids. The positive plasmids were selected by double digestion and PCR, and then sequenced. Finally, the structure and function of the sequence obtained were predicted by bioinformatics methods. [Results] The RPO30 gene was successfully obtained; its ORF was 585 bp, encoding 193 amino acids and containing a recognition site for Hind III. Moreover, the SPPV RPO30 gene shared different homologies with the RPO30 gene sequences of other pox virus strains from GenBank database. Further analysis by biological software showed that in RPO30 protein, amino acids 4-12, 18-26, 50- 61, 68- 92 and 176-190 had a high possibility to form the active center, and acting to these regions was likely to inactivate the enzyme encoded by the sequence, thus to inhibit viral replication efficiently. [Conclusion] This study will lay foundation for further study on the structure and function of RPO30.展开更多
基金Supported by Science and Technology Program of Shandong Province (No. 2010GHY10501)National Department Public Benefit Research Fond of China (No. 200909020)~~
文摘RpoS protein is a σ factor of RNA polymerase that can control the expression of a group-specific gene, thus playing a vital role in bacteria. In bacteria, RpoS expression is under strict control and is mainly regulated at three levels： transcription level, translation level and post-translational level. Environmental stress enters bacterial cells through signal transduction and leads to a series of variations in microenvironment, thereby causing changes of regulator and controlling its levels based on the direct and indirect interaction between regulator and RpoS protein. In addition, RpoS protein has played special roles in bacteria, therefore the changes of RpoS protein levels will lead to variations in expression levels of a large number of genes, thereby causing variations of bacterial response to different environmental stress and changes of certain characteristics of bacteria, which provides a new strategy for the control of bacterial diseases in the future. This paper reviewed the recent progress on the regulation of RpoS protein expression and its function in several common bacteria. Due to the functional complexity of RpoS protein, there are still a lot of unknown functions to be further identified.
基金Supported by the National Natural Science Foundation of China(31001056)the National Natural Science Foundation of China(31101802)+1 种基金Major Program for New Transgenic Organism Verities Breeding of Ministry of Agriculture of China(2009ZX08008-010B)Key Science and Technology Foundation of Gansu Province(092NKDA032)~~
文摘[Objective] The study aimed to clone RPO30 gene from Sheeppox virus （SPPV） and predict the structure and function of the sequence. [Method] RPO30 gene of SPPV was cloned with PCR, linked into pMD18-T simple vector and then transformed into E. coli DH5a. In blue-white screen, the white colonies were selected to prepare plasmids. The positive plasmids were selected by double digestion and PCR, and then sequenced. Finally, the structure and function of the sequence obtained were predicted by bioinformatics methods. [Results] The RPO30 gene was successfully obtained; its ORF was 585 bp, encoding 193 amino acids and containing a recognition site for Hind III. Moreover, the SPPV RPO30 gene shared different homologies with the RPO30 gene sequences of other pox virus strains from GenBank database. Further analysis by biological software showed that in RPO30 protein, amino acids 4-12, 18-26, 50- 61, 68- 92 and 176-190 had a high possibility to form the active center, and acting to these regions was likely to inactivate the enzyme encoded by the sequence, thus to inhibit viral replication efficiently. [Conclusion] This study will lay foundation for further study on the structure and function of RPO30.
