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Solution Structure and Dynamics of the Small Protein HVO_2922 from Haloferax volcanii
Author(s) -
Kubatova Nina,
Jonker Hendrik R. A.,
Saxena Krishna,
Richter Christian,
Vogel Verena,
Schreiber Sandra,
Marchfelder Anita,
Schwalbe Harald
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900085
Subject(s) - haloferax volcanii , haloarchaea , proteome , archaea , biology , biochemistry , mutagenesis , dimer , protein structure , chemistry , mutant , gene , organic chemistry
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, thus 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 protein stability and most likely for its functionality, as mutagenesis at the dimer interface leads to a decrease in stability and protein aggregation.