Nuclear-accumulation kinetics of p(9CksHs1) and p(9CksHs2) in live plant cells correlate with immunochemical characteristics

E. A. Williams; P. K. Hepler; A. C. Carrello; P. C.L. John

doi:10.1007/BF01294717

Nuclear-accumulation kinetics of p(9CksHs1) and p(9CksHs2) in live plant cells correlate with immunochemical characteristics

E. A. Williams^*, P. K. Hepler, A. C. Carrello, P. C.L. John

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

The two human homologues of the fission yeast cell cycle protein p13(suc1) displayed structural characteristics consistent with their existing in solution as differently folded monomers despite 81% identity with respect to their primary structures and both being capable of fulfilling the functions of their homologues in fission and budding yeasts. Carboxyfluorescein-labelled p(9CksHs1) and p(9CksH2) retained their native structures. When microinjected into live stamen hair cells of Tradescantia virginiana, the labelled proteins accumulated in the nuclei of the cells. Markedly different nuclear-accumulation kinetics indicated that the human proteins interact differently with other cellular constituents, which supports the proposition that they may have different roles in cellular regulation.

Original language	English
Pages (from-to)	98-105
Number of pages	8
Journal	Protoplasma
Volume	207
Issue number	1-2
DOIs	https://doi.org/10.1007/BF01294717
Publication status	Published - 1999

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title = "Nuclear-accumulation kinetics of p(9CksHs1) and p(9CksHs2) in live plant cells correlate with immunochemical characteristics",

abstract = "The two human homologues of the fission yeast cell cycle protein p13(suc1) displayed structural characteristics consistent with their existing in solution as differently folded monomers despite 81% identity with respect to their primary structures and both being capable of fulfilling the functions of their homologues in fission and budding yeasts. Carboxyfluorescein-labelled p(9CksHs1) and p(9CksH2) retained their native structures. When microinjected into live stamen hair cells of Tradescantia virginiana, the labelled proteins accumulated in the nuclei of the cells. Markedly different nuclear-accumulation kinetics indicated that the human proteins interact differently with other cellular constituents, which supports the proposition that they may have different roles in cellular regulation.",

keywords = "Cell division, Nucleus, P(9CksHs1), P(9CksHs2), P13(suc1), Tradescantia virginiana",

author = "Williams, {E. A.} and Hepler, {P. K.} and Carrello, {A. C.} and John, {P. C.L.}",

year = "1999",

doi = "10.1007/BF01294717",

language = "English",

volume = "207",

pages = "98--105",

journal = "Protoplasma",

issn = "0033-183X",

publisher = "Springer-Verlag Wien",

number = "1-2",

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TY - JOUR

T1 - Nuclear-accumulation kinetics of p(9CksHs1) and p(9CksHs2) in live plant cells correlate with immunochemical characteristics

AU - Williams, E. A.

AU - Hepler, P. K.

AU - Carrello, A. C.

AU - John, P. C.L.

PY - 1999

Y1 - 1999

N2 - The two human homologues of the fission yeast cell cycle protein p13(suc1) displayed structural characteristics consistent with their existing in solution as differently folded monomers despite 81% identity with respect to their primary structures and both being capable of fulfilling the functions of their homologues in fission and budding yeasts. Carboxyfluorescein-labelled p(9CksHs1) and p(9CksH2) retained their native structures. When microinjected into live stamen hair cells of Tradescantia virginiana, the labelled proteins accumulated in the nuclei of the cells. Markedly different nuclear-accumulation kinetics indicated that the human proteins interact differently with other cellular constituents, which supports the proposition that they may have different roles in cellular regulation.

AB - The two human homologues of the fission yeast cell cycle protein p13(suc1) displayed structural characteristics consistent with their existing in solution as differently folded monomers despite 81% identity with respect to their primary structures and both being capable of fulfilling the functions of their homologues in fission and budding yeasts. Carboxyfluorescein-labelled p(9CksHs1) and p(9CksH2) retained their native structures. When microinjected into live stamen hair cells of Tradescantia virginiana, the labelled proteins accumulated in the nuclei of the cells. Markedly different nuclear-accumulation kinetics indicated that the human proteins interact differently with other cellular constituents, which supports the proposition that they may have different roles in cellular regulation.

KW - Cell division

KW - Nucleus

KW - P(9CksHs1)

KW - P(9CksHs2)

KW - P13(suc1)

KW - Tradescantia virginiana

UR - http://www.scopus.com/inward/record.url?scp=0032988342&partnerID=8YFLogxK

U2 - 10.1007/BF01294717

DO - 10.1007/BF01294717

M3 - Article

SN - 0033-183X

VL - 207

SP - 98

EP - 105

JO - Protoplasma

JF - Protoplasma

IS - 1-2

ER -

Nuclear-accumulation kinetics of p(9CksHs1) and p(9CksHs2) in live plant cells correlate with immunochemical characteristics

Abstract

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