Actin: A Dynamic Framework for Multiple Plant Cell Functions by Richard B. Meagher, Elizabeth C. McKinney (auth.), C. J.

By Richard B. Meagher, Elizabeth C. McKinney (auth.), C. J. Staiger, F. Baluška, D. Volkmann, P. W. Barlow (eds.)

Actin is a very ample protein that includes a dynamic polymeric community found in all eukaryotic cells, referred to as the actin cytoskeleton. The constitution and serve as of the actin cytoskeleton, that's modulated by way of a plethora of actin-binding proteins, plays a various variety of mobile roles. Well-documented features for actin comprise: supplying the molecular tracks for cytoplasmic streaming and organelle activities; formation of tethers that advisor the mobile plate to the department web site in the course of cytokinesis; production of honeycomb-like arrays that enmesh and immobilize plastids in distinct subcellular styles; aiding the vesicle site visitors and cytoplasmic association crucial for the directional secretory mechanism that underpins tip development of yes cells; and coordinating the flowery cytoplasmic responses to additional- and intracellular signs. the former 20 years have witnessed an incredible accumulation of knowledge in relation to the mobile, biochemical, and molecular features of some of these primary mobile techniques. This caused the editors to place jointly a various number of subject matters, contributed by means of verified foreign specialists, on the topic of the plant actin cytoskeleton. as the actin cytoskeleton impinges on a mess of approaches serious for plant development and improvement, in addition to for responses to the surroundings, the ebook should be helpful to any researcher, from the complex undergraduate to the senior investigator, who's drawn to those parts of plant telephone biology.

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Extra resources for Actin: A Dynamic Framework for Multiple Plant Cell Functions

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AtMYA3 contains a very similar motor-domain sequence (70% identical) to AtMYA1 and AtMYA2 followed 33 2. Myosins by a neck region with five IQ motifs which is unusual because it also contains a motif for a consensus nucleotide binding site. D) Figure 2. The plant myosin sequence names, accession numbers, date of submission and their sizes. This lists all the full length plant myosin sequences available so far. , 1994). Those names have been kept in the nomenclature and have only been supplemented with the initials for the plant species they have been isolated from.

These AtATM 1 tail regions are similar to those in the other myosins of class VIII such as AtATM2, HaMYO 1, ZmZMM3 and AtVIII-A and AtVIII-B, and are unique to the class VIII myosins since they do not show any 38 Reichelt and Kendrick-Jones homologies with other myosin classes or other non-myosin proteins. , 1999) is thought to be specific for the class VIII myosins. In cell extracts, this antibody cross-reacts with polypeptides of 130 kDa, which confirms the predicted molecular weight of the class VIII myosin-I , AtATMl.

1994). Class XI also contains three Helianthus myosins HaMY02, HaMY04 and HaMY05 (Vugrek & Menzel, 1997, unpublished results), two Zea myosins, ZmMYOl and ZmMy02, one Chlamydomonas myosin CrMYO 1, and further nine Arabidopsis myosin sequences which have been identified by the Genome Sequencing Project (AtXI-A to AtXI-B). AtMYA3 is closely related, but not identical, to AtXI-B, but because its core domain is not full length, AtMYA3 has not been included in the phylogenetic tree. Interestingly, AtXI-D, AtXI-E, and AtXI-I contain a leucine zipper motif (prosite motif PS00029) in their Cterminal tails which could be involved in dimerization.

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