@article{
 title = {Expression and purification of untagged Glnk proteins from actinobacteria},
 type = {article},
 year = {2017},
 identifiers = {[object Object]},
 keywords = {Actinobacteria,CD analysis,GlnK,PII},
 pages = {949-958},
 volume = {16},
 id = {78a0823c-35a1-3fa5-893e-c49efbab6702},
 created = {2019-02-04T15:29:29.330Z},
 file_attached = {false},
 profile_id = {81a97cb0-31b8-3385-bd0e-efcfffedaada},
 group_id = {b954b4a7-36ce-39f9-9501-2e3795a979e9},
 last_modified = {2019-02-04T15:29:29.330Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {Gerhardt2017},
 source_type = {article},
 language = {eng},
 notes = {CAPES qualis 2013-2016 CB I: B3},
 private_publication = {false},
 abstract = {The PII protein family constitutes one of the most conserved and well distributed family of signal transduction proteins in nature. These proteins play key roles in nitrogen and carbon metabolism. PII function has been well documented in Gram-negative bacteria. However, there are very few reports describing the in vitro properties and function of PII derived from Gram-positive bacteria. Here we present the heterologous expression and efficient purification protocols for untagged PII from three Actinobacteria of medical and biotechnological interest namely: Mycobacterium tuberculosis, Rhodococcus jostii and Streptomyces coelicolor. Circular dichroism and gel filtration analysis supported that the purified proteins are correctly folded. The purification protocol described here will facilitate biochemical studies and help to uncover the biochemical functions of PII proteins in Actinobacteria.},
 bibtype = {article},
 author = {Gerhardt, Edileusa C.M. and Moure, Vivian R. and Souza, Andrey W. and Pedrosa, Fabio O. and Souza, Emanuel M. and Diacovich, Lautaro and Gramajo, Hugo and Huergo, Luciano F.},
 journal = {EXCLI Journal}
}

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