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The Role of Importin-s in Nuclear Envelope Assembly.

紀錄類型:	書目-語言資料,手稿 : Monograph/item
正題名/作者:	The Role of Importin-s in Nuclear Envelope Assembly./
作者:	Timinszky, Gyula.
面頁冊數:	1 online resource (47 pages)
附註:	Source: Dissertations Abstracts International, Volume: 85-06, Section: B.
Contained By:	Dissertations Abstracts International85-06B.
標題:	Genetics. -
電子資源:	click for full text (PQDT)
ISBN:	9798381045260

The Role of Importin-s in Nuclear Envelope Assembly.
Timinszky, Gyula.

The Role of Importin-s in Nuclear Envelope Assembly. - 1 online resource (47 pages)

Source: Dissertations Abstracts International, Volume: 85-06, Section: B.

Thesis (Ph.D.)--Szeged University (Hungary), 2003.

Includes bibliographical references

Three of the four independently induced KetelD dominant negative female sterile mutations, that identify the Drosophila importin-P gene, originated due to C4114 -»T transition and the concurrent replacement of proline446 by leucine (P446L-imp-P). The above-mentioned KetelD mutations abolish RanGTP binding of P446L-imp-P and result in increased RanGDP binding ability. P446L-imp-P does not exert its dominant negative effect on nuclear protein import and has basically no effect on mitotic spindle-related functions and chromosome segregation. However, it interferes with nuclear envelope (NE) assembly during the mitosis-to-interphase transition, revealing a novel function of importin-p. Along elucidating the mode of action of P446L-imp-P we studied in vitro NE assembly on Sepharose beads. While Drosophila embryo extracts support NE assembly over Sepharose beads coated with Ran, NE assembly - like in the KetelDeggs - does not take place in extracts supplied with exogenous P446L-imp-p. NE also forms over importin-P coated beads. Surprisingly, when immobilized to Sepharose beads P446L-imp-P as efficiently recruit NE vesicles as normal importin-p. The discrepancy in behavior of cytoplasmic and bead bound P446L-imp-p appears to be related to its increased microtubule (MT) binding ability as compared to normal importin-p. While wild type importin-P is able to bind to MTs and the binding ceases upon RanGTP interaction, P446Limp-P cannot be removed from the MTs by RanGTP. P446L-imp-P, like normal importin-P, binds some types of the nucleoporins that have been known to be required for NE assembly at the end of mitosis. It appears that the inhibitory effect of P446L-imp-P on NE assembly is caused by sequestering to the MTs some of the nuclear pore complex (NPC) proteins (nucleoporins) required for NE assembly.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2024

Mode of access: World Wide Web

ISBN: 9798381045260Subjects--Topical Terms:

578972
Genetics.
Index Terms--Genre/Form:

554714
Electronic books.

The Role of Importin-s in Nuclear Envelope Assembly.
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520 $a Three of the four independently induced KetelD dominant negative female sterile mutations, that identify the Drosophila importin-P gene, originated due to C4114 -»T transition and the concurrent replacement of proline446 by leucine (P446L-imp-P). The above-mentioned KetelD mutations abolish RanGTP binding of P446L-imp-P and result in increased RanGDP binding ability. P446L-imp-P does not exert its dominant negative effect on nuclear protein import and has basically no effect on mitotic spindle-related functions and chromosome segregation. However, it interferes with nuclear envelope (NE) assembly during the mitosis-to-interphase transition, revealing a novel function of importin-p. Along elucidating the mode of action of P446L-imp-P we studied in vitro NE assembly on Sepharose beads. While Drosophila embryo extracts support NE assembly over Sepharose beads coated with Ran, NE assembly - like in the KetelDeggs - does not take place in extracts supplied with exogenous P446L-imp-p. NE also forms over importin-P coated beads. Surprisingly, when immobilized to Sepharose beads P446L-imp-P as efficiently recruit NE vesicles as normal importin-p. The discrepancy in behavior of cytoplasmic and bead bound P446L-imp-p appears to be related to its increased microtubule (MT) binding ability as compared to normal importin-p. While wild type importin-P is able to bind to MTs and the binding ceases upon RanGTP interaction, P446Limp-P cannot be removed from the MTs by RanGTP. P446L-imp-P, like normal importin-P, binds some types of the nucleoporins that have been known to be required for NE assembly at the end of mitosis. It appears that the inhibitory effect of P446L-imp-P on NE assembly is caused by sequestering to the MTs some of the nuclear pore complex (NPC) proteins (nucleoporins) required for NE assembly.
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