Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이진원 | - |
dc.date.accessioned | 2019-12-01T15:56:38Z | - |
dc.date.available | 2019-12-01T15:56:38Z | - |
dc.date.issued | 2017-10 | - |
dc.identifier.citation | JOURNAL OF MICROBIOLOGY, v. 55, no. 10, page. 816-822 | en_US |
dc.identifier.issn | 1225-8873 | - |
dc.identifier.issn | 1976-3794 | - |
dc.identifier.uri | https://link.springer.com/article/10.1007%2Fs12275-017-7266-x | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/115990 | - |
dc.description.abstract | The Escherichia coli cAMP receptor protein (CRP) utili7Ps the helix-turn-helix motif for DNA binding. The CRP's recognition helix, termed F-helix, includes a stretch of six amino acids (Arg180, G1u181, Thr182, Va1183, G1y184, and Arg185) for direct DNA contacts. Arg180, G1u181 and Arg185 are known as important residues for DNA binding and specificity, but little has been studied for the other residues. Here we show that G1y184 is another F-helix residue critical for the transcriptional activation function of CRP. First, glycine was repeatedly selected at CRP position 184 for its unique ability to provide wild type-level transcriptional activation activity. To dissect the glycine requirement, wild type CRP and mutants G184A, G184F, G184S, and G184Y were purified and their in vitro DNA-binding activity was measured. G184A and G184F displayed reduced DNA binding, which may explain their low transcriptional activation activity. However, G184S and G184Y displayed apparently normal DNA affinity. Therefore, an additional factor is needed to account for the diminished transcriptional activation function in G184S and G184Y, and the best explanation is perturbations in their interaction with RNA polymerase. The fact that glycine is the smallest amino acid could not fully warrant its suitability, as shown in this study. We hypothesize that G1y184 fulfills the dual functions of DNA binding and RNA polymerase interaction by conferring conformational flexibility to the F-helix. | en_US |
dc.description.sponsorship | This work was supported by National Institutes of Health Grant R15AI101919 from the NIAID (to H. Y.). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. We would also like to thank Samyuktha Dasari and Andres Nevarez for technical support. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | MICROBIOLOGICAL SOCIETY KOREA | en_US |
dc.subject | CRP | en_US |
dc.subject | Escherichia coli | en_US |
dc.subject | Glyl 84 | en_US |
dc.subject | DNA binding | en_US |
dc.subject | transcriptional activation | en_US |
dc.subject | conformational flexibility | en_US |
dc.title | G1y184 of the Escherichia coli cAMP receptor protein provides optimal context for both DNA binding and RNA polymerase interaction | en_US |
dc.type | Article | en_US |
dc.relation.no | 10 | - |
dc.relation.volume | 55 | - |
dc.identifier.doi | 10.1007/s12275-017-7266-x | - |
dc.relation.page | 816-822 | - |
dc.relation.journal | JOURNAL OF MICROBIOLOGY | - |
dc.contributor.googleauthor | Hicks, Matt N. | - |
dc.contributor.googleauthor | Gunasekara, Sanjiva | - |
dc.contributor.googleauthor | Serate, Jose | - |
dc.contributor.googleauthor | Park, Jin | - |
dc.contributor.googleauthor | Mosharaf, Pegah | - |
dc.contributor.googleauthor | Zhou, Yue | - |
dc.contributor.googleauthor | Lee, Jin-Won | - |
dc.contributor.googleauthor | Youn, Hwan | - |
dc.relation.code | 2017008723 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF NATURAL SCIENCES[S] | - |
dc.sector.department | DEPARTMENT OF LIFE SCIENCE | - |
dc.identifier.pid | jwl | - |
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