The human recombinant TSR2 protein is typically expressed in Escherichia coli (E. coli) and is often tagged with a His-tag at the N-terminus to facilitate purification . The recombinant protein corresponds to the amino acids 1-190 of the human TSR2 sequence . The theoretical molecular weight of TSR2 is approximately 23.2 kDa, although the observed molecular weight may vary due to post-translational modifications and other experimental factors .
TSR2 is involved in the processing of 20S pre-rRNA, a precursor to the 18S rRNA, which is a component of the small subunit of the ribosome . Proper processing of pre-rRNA is essential for the assembly of functional ribosomes and, consequently, for efficient protein synthesis. Disruptions in rRNA processing can lead to defects in ribosome assembly and function, which can have wide-ranging effects on cellular physiology.
While specific tissue distribution data for TSR2 is limited, its role in ribosome biogenesis suggests that it is likely to be expressed in all actively dividing cells, as these cells require a high rate of protein synthesis. This includes tissues with high cellular turnover, such as the bone marrow, gastrointestinal tract, and developing tissues.
The expression and activity of TSR2 are likely regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational mechanisms. Given its essential role in ribosome biogenesis, TSR2 expression is probably tightly controlled to ensure proper cellular function and to respond to changes in cellular growth and proliferation demands.
Recombinant human TSR2 is used in various research applications to study ribosome biogenesis and rRNA processing. It can be utilized in biochemical assays, structural studies, and functional analyses to understand its role in ribosome assembly and its potential implications in diseases related to ribosome dysfunction.