author_facet POKORNÁ, J.
SCHWARZEROVÁ, K.
ZELENKOVÁ, S.
PETRÁŠEK, J.
JANOTOVÁ, I.
ČAPKOVÁ, V.
OPATRNÝ, Z.
POKORNÁ, J.
SCHWARZEROVÁ, K.
ZELENKOVÁ, S.
PETRÁŠEK, J.
JANOTOVÁ, I.
ČAPKOVÁ, V.
OPATRNÝ, Z.
author POKORNÁ, J.
SCHWARZEROVÁ, K.
ZELENKOVÁ, S.
PETRÁŠEK, J.
JANOTOVÁ, I.
ČAPKOVÁ, V.
OPATRNÝ, Z.
spellingShingle POKORNÁ, J.
SCHWARZEROVÁ, K.
ZELENKOVÁ, S.
PETRÁŠEK, J.
JANOTOVÁ, I.
ČAPKOVÁ, V.
OPATRNÝ, Z.
Plant, Cell & Environment
Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
Plant Science
Physiology
author_sort pokorná, j.
spelling POKORNÁ, J. SCHWARZEROVÁ, K. ZELENKOVÁ, S. PETRÁŠEK, J. JANOTOVÁ, I. ČAPKOVÁ, V. OPATRNÝ, Z. 0140-7791 1365-3040 Wiley Plant Science Physiology http://dx.doi.org/10.1111/j.1365-3040.2004.01186.x <jats:title>ABSTRACT</jats:title><jats:p>Cytoskeletal proteins assemble into dynamic polymers that play many roles in nuclear and cell division, signal transduction, and determination of cell shape and polarity. The distribution and dynamics of microtubules (MTs) and actin filaments (AFs) are determined, among other factors, by the location of their nucleation sites. Whereas the sites of microtubule nucleation in plants are known to be located under the plasma membrane and on the nuclear envelope during interphase, there is a striking lack of information about nucleation sites of AFs. In the studies reported herein, low temperature (0 °C) was used to de‐polymerize AFs and MTs in tobacco BY‐2 (<jats:italic>Nicotiana tabacum</jats:italic> L.) cells at interphase. The extent of de‐polymerization of cytoskeletal filaments in interphase cells during cold treatment and the subcellular distribution of nucleation sites during subsequent recovery at 25 °C were monitored by means of fluorescence microscopy. The results show that AFs re‐polymerized rapidly from sites located in the cortical region and on the nuclear envelope, similarly to the initiation sites of MTs. In contrast to MTs, however, complete reconstitution of AFs was preceded by the formation of transient actin structures including actin dots, rods, and filaments with a dotted signal. Immunoblotting of soluble and sedimentable protein fractions showed no changes in the relative amounts of free and membrane‐bound actin or tubulin.</jats:p> Sites of actin filament initiation and reorganization in cold‐treated tobacco cells Plant, Cell & Environment
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source_id 49
title Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_unstemmed Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_full Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_fullStr Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_full_unstemmed Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_short Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_sort sites of actin filament initiation and reorganization in cold‐treated tobacco cells
topic Plant Science
Physiology
url http://dx.doi.org/10.1111/j.1365-3040.2004.01186.x
publishDate 2004
physical 641-653
description <jats:title>ABSTRACT</jats:title><jats:p>Cytoskeletal proteins assemble into dynamic polymers that play many roles in nuclear and cell division, signal transduction, and determination of cell shape and polarity. The distribution and dynamics of microtubules (MTs) and actin filaments (AFs) are determined, among other factors, by the location of their nucleation sites. Whereas the sites of microtubule nucleation in plants are known to be located under the plasma membrane and on the nuclear envelope during interphase, there is a striking lack of information about nucleation sites of AFs. In the studies reported herein, low temperature (0 °C) was used to de‐polymerize AFs and MTs in tobacco BY‐2 (<jats:italic>Nicotiana tabacum</jats:italic> L.) cells at interphase. The extent of de‐polymerization of cytoskeletal filaments in interphase cells during cold treatment and the subcellular distribution of nucleation sites during subsequent recovery at 25 °C were monitored by means of fluorescence microscopy. The results show that AFs re‐polymerized rapidly from sites located in the cortical region and on the nuclear envelope, similarly to the initiation sites of MTs. In contrast to MTs, however, complete reconstitution of AFs was preceded by the formation of transient actin structures including actin dots, rods, and filaments with a dotted signal. Immunoblotting of soluble and sedimentable protein fractions showed no changes in the relative amounts of free and membrane‐bound actin or tubulin.</jats:p>
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author POKORNÁ, J., SCHWARZEROVÁ, K., ZELENKOVÁ, S., PETRÁŠEK, J., JANOTOVÁ, I., ČAPKOVÁ, V., OPATRNÝ, Z.
author_facet POKORNÁ, J., SCHWARZEROVÁ, K., ZELENKOVÁ, S., PETRÁŠEK, J., JANOTOVÁ, I., ČAPKOVÁ, V., OPATRNÝ, Z., POKORNÁ, J., SCHWARZEROVÁ, K., ZELENKOVÁ, S., PETRÁŠEK, J., JANOTOVÁ, I., ČAPKOVÁ, V., OPATRNÝ, Z.
author_sort pokorná, j.
container_issue 5
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container_title Plant, Cell & Environment
container_volume 27
description <jats:title>ABSTRACT</jats:title><jats:p>Cytoskeletal proteins assemble into dynamic polymers that play many roles in nuclear and cell division, signal transduction, and determination of cell shape and polarity. The distribution and dynamics of microtubules (MTs) and actin filaments (AFs) are determined, among other factors, by the location of their nucleation sites. Whereas the sites of microtubule nucleation in plants are known to be located under the plasma membrane and on the nuclear envelope during interphase, there is a striking lack of information about nucleation sites of AFs. In the studies reported herein, low temperature (0 °C) was used to de‐polymerize AFs and MTs in tobacco BY‐2 (<jats:italic>Nicotiana tabacum</jats:italic> L.) cells at interphase. The extent of de‐polymerization of cytoskeletal filaments in interphase cells during cold treatment and the subcellular distribution of nucleation sites during subsequent recovery at 25 °C were monitored by means of fluorescence microscopy. The results show that AFs re‐polymerized rapidly from sites located in the cortical region and on the nuclear envelope, similarly to the initiation sites of MTs. In contrast to MTs, however, complete reconstitution of AFs was preceded by the formation of transient actin structures including actin dots, rods, and filaments with a dotted signal. Immunoblotting of soluble and sedimentable protein fractions showed no changes in the relative amounts of free and membrane‐bound actin or tubulin.</jats:p>
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spelling POKORNÁ, J. SCHWARZEROVÁ, K. ZELENKOVÁ, S. PETRÁŠEK, J. JANOTOVÁ, I. ČAPKOVÁ, V. OPATRNÝ, Z. 0140-7791 1365-3040 Wiley Plant Science Physiology http://dx.doi.org/10.1111/j.1365-3040.2004.01186.x <jats:title>ABSTRACT</jats:title><jats:p>Cytoskeletal proteins assemble into dynamic polymers that play many roles in nuclear and cell division, signal transduction, and determination of cell shape and polarity. The distribution and dynamics of microtubules (MTs) and actin filaments (AFs) are determined, among other factors, by the location of their nucleation sites. Whereas the sites of microtubule nucleation in plants are known to be located under the plasma membrane and on the nuclear envelope during interphase, there is a striking lack of information about nucleation sites of AFs. In the studies reported herein, low temperature (0 °C) was used to de‐polymerize AFs and MTs in tobacco BY‐2 (<jats:italic>Nicotiana tabacum</jats:italic> L.) cells at interphase. The extent of de‐polymerization of cytoskeletal filaments in interphase cells during cold treatment and the subcellular distribution of nucleation sites during subsequent recovery at 25 °C were monitored by means of fluorescence microscopy. The results show that AFs re‐polymerized rapidly from sites located in the cortical region and on the nuclear envelope, similarly to the initiation sites of MTs. In contrast to MTs, however, complete reconstitution of AFs was preceded by the formation of transient actin structures including actin dots, rods, and filaments with a dotted signal. Immunoblotting of soluble and sedimentable protein fractions showed no changes in the relative amounts of free and membrane‐bound actin or tubulin.</jats:p> Sites of actin filament initiation and reorganization in cold‐treated tobacco cells Plant, Cell & Environment
spellingShingle POKORNÁ, J., SCHWARZEROVÁ, K., ZELENKOVÁ, S., PETRÁŠEK, J., JANOTOVÁ, I., ČAPKOVÁ, V., OPATRNÝ, Z., Plant, Cell & Environment, Sites of actin filament initiation and reorganization in cold‐treated tobacco cells, Plant Science, Physiology
title Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_full Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_fullStr Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_full_unstemmed Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_short Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_sort sites of actin filament initiation and reorganization in cold‐treated tobacco cells
title_unstemmed Sites of actin filament initiation and reorganization in cold‐treated tobacco cells
topic Plant Science, Physiology
url http://dx.doi.org/10.1111/j.1365-3040.2004.01186.x