Structural highlights
Publication Abstract from PubMed
Past sequencing campaigns overlooked small proteins as they seemed to be irrelevant due to their small size. However, their occurrence is widespread and there is growing evidence that these small proteins are in fact functionally very important in organisms found in all kingdoms of life. Within a global proteome analysis for small proteins of the archaeal model organism Haloferax volcanii, the HVO_2922 protein has been identified. It is differentially expressed in response to changes in iron and salt concentrations, suggesting that its expression is stress-regulated. The protein is conserved among Haloarchaea and contains an uncharacterized domain of unknown function (DUF1508, UPF0339 family protein). We elucidated the NMR solution structure, which shows that the isolated protein forms a symmetrical dimer. The dimerization is found to be concentration-dependent and essential for the protein stability and most likely for its functionality as mutagenesis at the dimer interface leads to a decrease of stability and protein aggregation.
Solution structure and dynamics of the small protein HVO_2922 from Haloferax volcanii.,Kubatova N, Jonker HRA, Saxena K, Richter C, Vogel V, Schreiber S, Marchfelder A, Schwalbe H Chembiochem. 2019 Jun 4. doi: 10.1002/cbic.201900085. PMID:31161645[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kubatova N, Jonker HRA, Saxena K, Richter C, Vogel V, Schreiber S, Marchfelder A, Schwalbe H. Solution structure and dynamics of the small protein HVO_2922 from Haloferax volcanii. Chembiochem. 2019 Jun 4. doi: 10.1002/cbic.201900085. PMID:31161645 doi:http://dx.doi.org/10.1002/cbic.201900085
