Dimorphic aggregation behavior of a fusion polypeptide incorporating a stable protein domain (EGFP) with an amyloidogenic sequence (retroCspA).
IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh
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| Title |
Dimorphic aggregation behavior of a fusion polypeptide incorporating a stable protein domain (EGFP) with an amyloidogenic sequence (retroCspA).
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| Creator |
Sharma, Swati
Guptasarma, Purnananda |
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| Subject |
QR Microbiology
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| Description |
We describe the behavior of a polypeptide consisting of the genetic fusion of a structurally stable single-domain protein, EGFP (an analog of the green fluorescent protein) with an amyloidogenic sequence, retroCspA (known to readily form amyloid fibrils). Refolding of the fusion protein through single-step removal of denaturant and salt results in precipitation into amyloid aggregates displaying fibrillar morphology, thioflavin T binding as well as green fluorescence. Refolding through step-wise reduction of denaturant concentration in the presence of salt yields a soluble aggregate containing a folded, thermally-stable, non-fluorescent EGFP domain. Together, these results indicate that retroCspA forces the fusion protein to aggregate; however, the EGFP domain remains folded in a native-like structural format in both soluble aggregates and precipitates.
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| Publisher |
Elsevier Science
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| Date |
2008-06-25
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://crdd.osdd.net/open/591/1/guptasarma08.15.pdf
Sharma, Swati and Guptasarma, Purnananda (2008) Dimorphic aggregation behavior of a fusion polypeptide incorporating a stable protein domain (EGFP) with an amyloidogenic sequence (retroCspA). FEBS letters, 582 (15). pp. 2203-11. ISSN 0014-5793 |
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| Relation |
http://www.febsletters.org/article/S0014-5793(08)00409-2/abstract
http://crdd.osdd.net/open/591/ |
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