S-adenosyl-L-homocysteine riboswitch | |
---|---|
![]() Predicted
secondary structure and
sequence conservation of SAH_riboswitch | |
Identifiers | |
Symbol | SAH_riboswitch |
Rfam | RF01057 |
Other data | |
RNA type | Cis-reg; riboswitch |
Domain(s) | Bacteria |
SO | SO:0005836 |
PDB structures | PDBe |
SAH riboswitches are a kind of riboswitch that bind S-adenosylhomocysteine (SAH). [1] When the coenzyme S-adenosylmethionine (SAM) is used in a methylation reaction, SAH is produced. SAH riboswitches typically up-regulate genes involved in recycling SAH to create more SAM (or the metabolically related methionine). This is particularly relevant to cells, because high levels of SAH can be toxic. [2] Originally identified by bioinformatics, [3] SAH riboswitches are apparent in many species of bacteria, predominantly certain Pseudomonadota and Actinomycetota. The atomic-resolution 3-dimensional structure of an SAH riboswitch has been solved using X-ray crystallography. [4]
S-adenosyl-L-homocysteine riboswitch | |
---|---|
![]() Predicted
secondary structure and
sequence conservation of SAH_riboswitch | |
Identifiers | |
Symbol | SAH_riboswitch |
Rfam | RF01057 |
Other data | |
RNA type | Cis-reg; riboswitch |
Domain(s) | Bacteria |
SO | SO:0005836 |
PDB structures | PDBe |
SAH riboswitches are a kind of riboswitch that bind S-adenosylhomocysteine (SAH). [1] When the coenzyme S-adenosylmethionine (SAM) is used in a methylation reaction, SAH is produced. SAH riboswitches typically up-regulate genes involved in recycling SAH to create more SAM (or the metabolically related methionine). This is particularly relevant to cells, because high levels of SAH can be toxic. [2] Originally identified by bioinformatics, [3] SAH riboswitches are apparent in many species of bacteria, predominantly certain Pseudomonadota and Actinomycetota. The atomic-resolution 3-dimensional structure of an SAH riboswitch has been solved using X-ray crystallography. [4]