author_facet Abel, Steffen
Theologis, Athanasios
Abel, Steffen
Theologis, Athanasios
author Abel, Steffen
Theologis, Athanasios
spellingShingle Abel, Steffen
Theologis, Athanasios
The Plant Journal
A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
Cell Biology
Plant Science
Genetics
author_sort abel, steffen
spelling Abel, Steffen Theologis, Athanasios 0960-7412 1365-313X Wiley Cell Biology Plant Science Genetics http://dx.doi.org/10.1046/j.1365-313x.1995.08010087.x <jats:p>The plant hormone, indoleacetic acid (IAA), transcriptionally activates two early genes in pea, <jats:italic>PS‐IAA4/5</jats:italic> and <jats:italic>PS‐IAA6</jats:italic>, that encode short‐lived nuclear proteins. The identification of the nuclear localization signals (NLS) in PS‐IAA4 and PS‐IAA6 using progressive deletion analysis and site‐directed mutagenesis is reported. A C‐terminal SV40‐type NLS is sufficient to direct the β‐glucuronidase reporter to the nucleus of transiently transformed tobacco protoplasts, but is dispensible for nuclear localization of both proteins. The dominant and essential NLS in PS‐IAA4 and PS‐IAA6 overlap with a bipartite basic motif which is polymorphic and conserved in related proteins from other plant species, having the consensus sequence (KKNEK)KR‐X(<jats:sub>24–71</jats:sub>)‐(RSXRK)/(RK/RK). Both basic elements of this motif in PS‐IAA4, (KR‐X<jats:sub>41</jats:sub>‐RSYRK), function interdependently as a bipartite NLS. However, in PS‐IAA6 (KKNEKKR‐X<jats:sub>36</jats:sub>‐RKK) the upstream element of the corresponding motif contains additional basic residues which allow its autonomous function as an SV40‐type monopartite NLS. The spacer‐length polymorphism, X(<jats:sub>24–70</jats:sub>), in respective bipartite NLS peptides of several PS‐IAA4‐like proteins from <jats:italic>Arabidopsis thaliana</jats:italic> does not affect nuclear targeting function. The structural and functional variation of the bipartite basic motif in PS‐IAA4‐like proteins supports the proposed integrated consensus of NLS.</jats:p> A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (<i>Pisum sativum</i>) The Plant Journal
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series The Plant Journal
source_id 49
title A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_unstemmed A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_full A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_fullStr A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_full_unstemmed A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_short A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_sort a polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to ps‐iaa4 from pea (<i>pisum sativum</i>)
topic Cell Biology
Plant Science
Genetics
url http://dx.doi.org/10.1046/j.1365-313x.1995.08010087.x
publishDate 1995
physical 87-96
description <jats:p>The plant hormone, indoleacetic acid (IAA), transcriptionally activates two early genes in pea, <jats:italic>PS‐IAA4/5</jats:italic> and <jats:italic>PS‐IAA6</jats:italic>, that encode short‐lived nuclear proteins. The identification of the nuclear localization signals (NLS) in PS‐IAA4 and PS‐IAA6 using progressive deletion analysis and site‐directed mutagenesis is reported. A C‐terminal SV40‐type NLS is sufficient to direct the β‐glucuronidase reporter to the nucleus of transiently transformed tobacco protoplasts, but is dispensible for nuclear localization of both proteins. The dominant and essential NLS in PS‐IAA4 and PS‐IAA6 overlap with a bipartite basic motif which is polymorphic and conserved in related proteins from other plant species, having the consensus sequence (KKNEK)KR‐X(<jats:sub>24–71</jats:sub>)‐(RSXRK)/(RK/RK). Both basic elements of this motif in PS‐IAA4, (KR‐X<jats:sub>41</jats:sub>‐RSYRK), function interdependently as a bipartite NLS. However, in PS‐IAA6 (KKNEKKR‐X<jats:sub>36</jats:sub>‐RKK) the upstream element of the corresponding motif contains additional basic residues which allow its autonomous function as an SV40‐type monopartite NLS. The spacer‐length polymorphism, X(<jats:sub>24–70</jats:sub>), in respective bipartite NLS peptides of several PS‐IAA4‐like proteins from <jats:italic>Arabidopsis thaliana</jats:italic> does not affect nuclear targeting function. The structural and functional variation of the bipartite basic motif in PS‐IAA4‐like proteins supports the proposed integrated consensus of NLS.</jats:p>
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author Abel, Steffen, Theologis, Athanasios
author_facet Abel, Steffen, Theologis, Athanasios, Abel, Steffen, Theologis, Athanasios
author_sort abel, steffen
container_issue 1
container_start_page 87
container_title The Plant Journal
container_volume 8
description <jats:p>The plant hormone, indoleacetic acid (IAA), transcriptionally activates two early genes in pea, <jats:italic>PS‐IAA4/5</jats:italic> and <jats:italic>PS‐IAA6</jats:italic>, that encode short‐lived nuclear proteins. The identification of the nuclear localization signals (NLS) in PS‐IAA4 and PS‐IAA6 using progressive deletion analysis and site‐directed mutagenesis is reported. A C‐terminal SV40‐type NLS is sufficient to direct the β‐glucuronidase reporter to the nucleus of transiently transformed tobacco protoplasts, but is dispensible for nuclear localization of both proteins. The dominant and essential NLS in PS‐IAA4 and PS‐IAA6 overlap with a bipartite basic motif which is polymorphic and conserved in related proteins from other plant species, having the consensus sequence (KKNEK)KR‐X(<jats:sub>24–71</jats:sub>)‐(RSXRK)/(RK/RK). Both basic elements of this motif in PS‐IAA4, (KR‐X<jats:sub>41</jats:sub>‐RSYRK), function interdependently as a bipartite NLS. However, in PS‐IAA6 (KKNEKKR‐X<jats:sub>36</jats:sub>‐RKK) the upstream element of the corresponding motif contains additional basic residues which allow its autonomous function as an SV40‐type monopartite NLS. The spacer‐length polymorphism, X(<jats:sub>24–70</jats:sub>), in respective bipartite NLS peptides of several PS‐IAA4‐like proteins from <jats:italic>Arabidopsis thaliana</jats:italic> does not affect nuclear targeting function. The structural and functional variation of the bipartite basic motif in PS‐IAA4‐like proteins supports the proposed integrated consensus of NLS.</jats:p>
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institution DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1
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spelling Abel, Steffen Theologis, Athanasios 0960-7412 1365-313X Wiley Cell Biology Plant Science Genetics http://dx.doi.org/10.1046/j.1365-313x.1995.08010087.x <jats:p>The plant hormone, indoleacetic acid (IAA), transcriptionally activates two early genes in pea, <jats:italic>PS‐IAA4/5</jats:italic> and <jats:italic>PS‐IAA6</jats:italic>, that encode short‐lived nuclear proteins. The identification of the nuclear localization signals (NLS) in PS‐IAA4 and PS‐IAA6 using progressive deletion analysis and site‐directed mutagenesis is reported. A C‐terminal SV40‐type NLS is sufficient to direct the β‐glucuronidase reporter to the nucleus of transiently transformed tobacco protoplasts, but is dispensible for nuclear localization of both proteins. The dominant and essential NLS in PS‐IAA4 and PS‐IAA6 overlap with a bipartite basic motif which is polymorphic and conserved in related proteins from other plant species, having the consensus sequence (KKNEK)KR‐X(<jats:sub>24–71</jats:sub>)‐(RSXRK)/(RK/RK). Both basic elements of this motif in PS‐IAA4, (KR‐X<jats:sub>41</jats:sub>‐RSYRK), function interdependently as a bipartite NLS. However, in PS‐IAA6 (KKNEKKR‐X<jats:sub>36</jats:sub>‐RKK) the upstream element of the corresponding motif contains additional basic residues which allow its autonomous function as an SV40‐type monopartite NLS. The spacer‐length polymorphism, X(<jats:sub>24–70</jats:sub>), in respective bipartite NLS peptides of several PS‐IAA4‐like proteins from <jats:italic>Arabidopsis thaliana</jats:italic> does not affect nuclear targeting function. The structural and functional variation of the bipartite basic motif in PS‐IAA4‐like proteins supports the proposed integrated consensus of NLS.</jats:p> A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (<i>Pisum sativum</i>) The Plant Journal
spellingShingle Abel, Steffen, Theologis, Athanasios, The Plant Journal, A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum), Cell Biology, Plant Science, Genetics
title A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_full A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_fullStr A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_full_unstemmed A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_short A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
title_sort a polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to ps‐iaa4 from pea (<i>pisum sativum</i>)
title_unstemmed A polymorphic bipartite motif signals nuclear targeting of early auxin‐inducible proteins related to PS‐IAA4 from pea (Pisum sativum)
topic Cell Biology, Plant Science, Genetics
url http://dx.doi.org/10.1046/j.1365-313x.1995.08010087.x