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Investigation of talin head-tail interactions

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Date Issued:
2009
Summary:
Talin is a ubiquitous, high-molecular-weight, flexible protein that plays a critical role in focal adhesions by activating, as well as connecting, integrins to the actin cytoskeleton. Talin's inactive auto-inhibitory state is speculated to be one of its modes of regulation inside the cell and is achieved through its head-tail interactions. In order to decipher the stability of this interaction, the head domain (residues 206-405) was cloned into a modified pET28m vector while the tail domains (residues 1654-2344 and 2225-2344) were cloned into the pET32a vector to obtain octa-histidine tagged and un-tagged peptide, respectively. Neither co-expression nor pull-down using the His-tagged head domain was successful in purifying a stable head-tail complex. Our results indicate rather weak interactions between the talin head and rod domains and hence, under our experimental conditions, do not lead to a stable auto-inhibitory complex that can be purified for further studies.
Title: Investigation of talin head-tail interactions.
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Name(s): Butyn, Amber.
Harriet L. Wilkes Honors College
Type of Resource: text
Genre: Thesis
Issuance: multipart monograph
Date Issued: 2009
Publisher: Florida Atlantic University
Physical Form: electronic
electronic resource
Extent: vi, 35 leaves : ill. (some col.) ; 29 cm.
Language(s): English
Summary: Talin is a ubiquitous, high-molecular-weight, flexible protein that plays a critical role in focal adhesions by activating, as well as connecting, integrins to the actin cytoskeleton. Talin's inactive auto-inhibitory state is speculated to be one of its modes of regulation inside the cell and is achieved through its head-tail interactions. In order to decipher the stability of this interaction, the head domain (residues 206-405) was cloned into a modified pET28m vector while the tail domains (residues 1654-2344 and 2225-2344) were cloned into the pET32a vector to obtain octa-histidine tagged and un-tagged peptide, respectively. Neither co-expression nor pull-down using the His-tagged head domain was successful in purifying a stable head-tail complex. Our results indicate rather weak interactions between the talin head and rod domains and hence, under our experimental conditions, do not lead to a stable auto-inhibitory complex that can be purified for further studies.
Identifier: 459787318 (oclc), 209984 (digitool), FADT209984 (IID), fau:1358 (fedora)
Note(s): by Amber Butyn.
Thesis (B.A.)--Florida Atlantic University, Honors College, 2009.
Bibliography: leaves 32-35.
Electronic reproduction. Boca Raton, Fla., 2009. Mode of access: World Wide Web.
Subject(s): Membrane proteins -- Structure-activity relationships
Cell membranes -- Physiology
Molecular biology
Cell interaction
Developmental cytology
Held by: FBoU FAUER
Persistent Link to This Record: http://purl.flvc.org/FAU/209984
Use and Reproduction: Copyright © is held by the author, with permission granted to Florida Atlantic University to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires permission of the copyright holder.
Host Institution: FAU

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