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Analysis of nuclear organization: Nu...

Damelin, Marc Issac.

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Analysis of nuclear organization: Nucleocytoplasmic transport and chromatin remodeling.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Analysis of nuclear organization: Nucleocytoplasmic transport and chromatin remodeling./
Author:	Damelin, Marc Issac.
Description:	228 p.
Notes:	Adviser: Pamela A. Silver.
Contained By:	Dissertation Abstracts International63-04B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3051140
ISBN:	0493656480

Analysis of nuclear organization: Nucleocytoplasmic transport and chromatin remodeling.
Damelin, Marc Issac.

Analysis of nuclear organization: Nucleocytoplasmic transport and chromatin remodeling. - 228 p.

Adviser: Pamela A. Silver.

Thesis (Ph.D.)--Harvard University, 2002.

The nuclear pore complex (NPC) mediates the transport of macromolecules between the nucleus and cytoplasm. To better understand the mechanism of translocation through the NPC, I analyzed interactions between transport receptors and the NPC proteins, as well as the structural organization of the NPC. To this end, I developed a method that allows the in situ detection of protein interactions in the budding yeast <italic>Saccharomyces cerevisiae</italic>. In this microscopy-based assay, protein interactions are probed by fluorescence resonance energy transfer (FRET) between the enhanced cyan and yellow fluorescent proteins (ECFP, EYFP) fused to the target proteins.

ISBN: 0493656480Subjects--Topical Terms:

1017686
Biology, Cell.

Analysis of nuclear organization: Nucleocytoplasmic transport and chromatin remodeling.
LDR:03372nam 2200325 a 45 001 927731
005 20110425
008 110425s2002 eng d
020 $a 0493656480
035 $a (UnM)AAI3051140
035 $a AAI3051140
040 $a UnM $c UnM
100 1 $a Damelin, Marc Issac. $3 1251294
245 1 0 $a Analysis of nuclear organization: Nucleocytoplasmic transport and chromatin remodeling.
300 $a 228 p.
500 $a Adviser: Pamela A. Silver.
500 $a Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1742.
502 $a Thesis (Ph.D.)--Harvard University, 2002.
520 $a The nuclear pore complex (NPC) mediates the transport of macromolecules between the nucleus and cytoplasm. To better understand the mechanism of translocation through the NPC, I analyzed interactions between transport receptors and the NPC proteins, as well as the structural organization of the NPC. To this end, I developed a method that allows the in situ detection of protein interactions in the budding yeast <italic>Saccharomyces cerevisiae</italic>. In this microscopy-based assay, protein interactions are probed by fluorescence resonance energy transfer (FRET) between the enhanced cyan and yellow fluorescent proteins (ECFP, EYFP) fused to the target proteins.
520 $a Translocation pathways were investigated by assessing the patterns of interactions between transport receptors (importins and exportins) and proteins of the NPC (nucleoporins, nups). A panel of yeast strains each expressing functional receptor-ECFP and nup-EYFP fusions was generated and analyzed for FRET. The importin Pse1/Kap121 and the exportin Msn5 were found to have some common and some specific points of contact in the NPC. Kap121-Nup interactions were also examined by a series of immunoprecipitation experiments. The results indicate that an importin and exportin have overlapping but distinct translocation pathways.
520 $a To study the structural organization of the NPC, FRET was measured between the fluorescent proteins expressed as fusions to distinct nucleoporins. Thirteen FRET interactions were identified; independent genetics experiments were consistent with the results. Analysis of the spatial requirements of the FRET signals demonstrated the specificity of the assay. A refined molecular model of the NPC is proposed based on the integration of the FRET results with existing data.
520 $a In a separate project, the function of the yeast chromatin-remodeling complex RSC was investigated. Rsc9 was identified as a novel RSC component and was further characterized. Genome-wide localization analysis indicated that the Rsc9 targets include genes regulated by stress; two stress treatments resulted in genome-wide changes in Rsc9 occupancy. Northern analysis further demonstrated that Rsc9 is involved in both the repression and activation of genes regulated by the TOR signaling pathway. The results illustrate the response of a chromatin-remodeling factor to signaling cascades and have implications for the mechanism of RSC function.
590 $a School code: 0084.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biophysics, General. $3 1019105
690 $a 0307
690 $a 0379
690 $a 0786
710 2 0 $a Harvard University. $3 528741
773 0 $t Dissertation Abstracts International $g 63-04B.
790 $a 0084
790 1 0 $a Silver, Pamela A., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3051140