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Riboswitches regulate the synthesis of proteins and are controlled by related compounds such as thiamine pyrophosphate.^[1] They are usually found within non-coding portions of messenger RNAs.^[1]Thiamine pyrophosphate is also known as TPP. TPP is essential in all three domains of life, including: bacteria, fungi, and plants. ^[1] They use this specific riboswitch to control genes that are in charge of synthesizing thiamine and any phosphorylated derivatives.^[1]TPP and its riboswitch work together to directly regulate the synthesis of a proteins related to TPP. ^[1]Thiamine pyrophosphate is the most widely distributed riboswitch of the metabolite-sensing RNA regulatory system. ^[1] The reason for this is because TPP is a form of vitamin B1, and vitamin B1 takes an essential part in many protein-catalyzed reactions; thus it is used quite often.

Function

Magnesium Link

PAPER CITATION: ^[2]

TPP Link

Disease

Structural highlights

TPP riboswitches were one of the first of several classes found to form successful interactions with negatively charged phosphate groups.^[1] TPP's pyrophosphate group is bound by a pair of Mg2+ ions, . ^[1] TPP's terminal phosphate group is coordinately bonded to both , but the thiazole-linked phosphate is only coordinately bonded to Mg2.^[1] Holding Mg1 in place are and they can be found within the region that previously was known for pyrophosphate recognition.^[1] Structures of proteins bound to TPP typically position Mg2+, Ca2+, or Mn2+ ions using charged amino acids, in a site equivalent.^[1] However, the TPP riboswitch is the only riboswitch that contains the Mg1 ion.^[1] A bivalent cation allows TPP to reach into the pyrophosphate-binding pocket.^[1] This in turn stabilizes the important tertiary interactions that are required for gene regulation, and supporting the use of Mg2+ for TPP binding in both bacterial and eukaryotic TPP riboswitches.^[1]

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