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Effects of manganese on the proteomic expression in Deinococcus radiodurans

The addition of Mn2¡Ï to stationary phase culture of Deinococcus radiodurans could induce further cell division. This type of cell division termed "Mn-induced Cell Division (Mn-CD)". The Mn-CD cells were less resistant to radiation, having smaller cell size, and forming less red-pigment. However, the activities of antioxidation enzymes such as superoxide dismutase (SOD) and catalase, were increased. No other divalent metal ions could cause Mn-CD. In this study, 2-D electrophoresis and Matrix Assisted Laser Desorption Ionization (MALDI) MASS were used to analyze the proteomic differences between Mn-CD and normal uninduced cells. The results showed that the expression of ribosomal proteins L20, L34, L35, chain 3 of the large ribosomal subunit, preprotein translocase (SecE subunit) and three hypothetical proteins (DR1423, DR1897 and one unidentified gene product), were pressed significantly in the cell culture when Mn2¡Ï were added. Since these ribosomal proteins are responsible for the synthesis of protein, it is clear that Mn2¡Ï could disturb the proteins synthesis in this bacterium. The addition of Mn2¡Ïcould also induce the expression of acetyl-CoA acetyltransferase, transcriptional regulator (TetR family), phosphinothricin acetyltransferase and three hypothetical proteins (DR0214, DR0296 and DRA0100). The functions of these hypothetical proteins were not known yet. In conclusion, it is true that Mn2¡Ï could alter the proteomic expression and some metabolic pathways in D. radiodurans.

Identiferoai:union.ndltd.org:NSYSU/oai:NSYSU:etd-0716102-204545
Date16 July 2002
CreatorsLi, Pei-I
ContributorsChan-Shing Lin, Chi-Hsin Hsu, Jong-Kang Liu
PublisherNSYSU
Source SetsNSYSU Electronic Thesis and Dissertation Archive
LanguageCholon
Detected LanguageEnglish
Typetext
Formatapplication/pdf
Sourcehttp://etd.lib.nsysu.edu.tw/ETD-db/ETD-search/view_etd?URN=etd-0716102-204545
Rightsoff_campus_withheld, Copyright information available at source archive

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