期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 103, 期 30, 页码 11334-11339出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0602839103
关键词
cyanobacteria; protease
Calcium ions are important to some prokaryotic cellular processes, such as heterocyst differentiation of cyanobacteria. Intracellular free Ca2+ concentration, [Ca2+](i), increases several fold in hetero-cysts and is regulated by CcbP, a Ca2+-binding protein found in heterocyst-forming cyanobacteria. We demonstrate here that CcbP is degraded by HetR, a serine-type protease that controls heterocyst differentiation. The degradation depends on Ca2+ and appears to be specific because HetR did not digest other tested proteins. CcbP was found to bind two Ca2+ per molecule with K-D values of 200 nM and 12.8 mu M. Degradation of CcbP releases bound Ca2+ that contributes significantly to the increase of [Ca2+](i) during the process of heterocyst differentiation in Anabaena sp. strain PCC 7120. We suggest that degradation of CcbP is a mechanism of positive autoregulation of HetR. The down-regulation of ccbP in differentiating cells and mature heterocysts, which also is critical to the regulation of [Ca2+](i), depends on NtcA. Coexpression of ntcA and a ccbP promoter-controlled gfp in Escherichia coli diminished production of GFP, and the decrease is enhanced by a-ketoglutarate. It was also found that NtcA could bind a fragment of the ccbP promoter containing an NtcA-binding sequence in a a-ketoglutarate-dependent fashion. Therefore, [Ca2+], is regulated by a collaboration of HetR and NtcA in heterocyst differentiation in Anabaena sp. strain PCC 7120.
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