Structure and Biological Function of the RNA Pyrophosphohydrolase BdRppH from Bdellovibrio bacteriovorus

Journal Article · Thu Jan 01 04:00:00 EST 2009 · Structure

DOI:https://doi.org/10.1016/j.str.2008.12.022· OSTI ID:980539

Messing, S; Gabelli, S; Liu, Q; Celesnik, H; Belasco, J; Pineiro, S; Amzel, L

Until recently, the mechanism of mRNA decay in bacteria was thought to be different from that of eukaryotes. This paradigm changed with the discovery that RppH (ORF176/NudH/YgdP), an Escherichia coli enzyme that belongs to the Nudix superfamily, is an RNA pyrophosphohydrolase that initiates mRNA decay by cleaving pyrophosphate from the 5?-triphosphate. Here we report the 1.9 A resolution structure of the Nudix hydrolase BdRppH from Bdellovibrio bacteriovorus, a bacterium that feeds on other Gram-negative bacteria. Based on the structure of the enzyme alone and in complex with GTP-Mg2+, we propose a mode of RNA binding similar to that of the nuclear decapping enzyme from Xenopus laevis, X29. In additional experiments, we show that BdRppH can indeed function in vitro and in vivo as an RNA pyrophosphohydrolase. These findings set the basis for the identification of possible decapping enzymes in other bacteria.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 980539
• Report Number(s): BNL--93457-2010-JA
• Journal Information: Structure, Journal Name: Structure Vol. 17
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
BACTERIA
BIOLOGICAL FUNCTIONS
DECAY
ENZYMES
ESCHERICHIA COLI
FUNCTIONS
HYDROLASES
IN VITRO
IN VIVO
PYROPHOSPHATES
RESOLUTION
RNA
national synchrotron light source