title: A subclass of myosin XI is associated with mitochondria, plastids, and the molecular chaperone subunit TCP-1alpha in maize.
abstract: The role and regulation of specific plant myosins in cyclosis is not well understood. In the present report, an affinity-purified antibody generated against a conserved tail region of some class XI plant myosin isoforms was used for biochemical and immunofluorescence studies of Zea mays. Myosin XI co-localized with plastids and mitochondria but not with nuclei, the Golgi apparatus, endoplasmic reticulum, or peroxisomes. This suggests that myosin XI is involved in the motility of specific organelles. Myosin XI was more than 50% co-localized with tailless complex polypeptide-1alpha (TCP-1alpha) in tissue sections of mature tissues located more than 1.0 mm from the apex, and the two proteins co-eluted from gel filtration and ion exchange columns. On Western blots, TCP-1alpha isoforms showed a developmental shift from the youngest 5.0 mm of the root to more mature regions that were more than 10.0 mm from the apex. This developmental shift coincided with a higher percentage of myosin XI /TCP-1alpha co-localization, and faster degradation of myosin XI by serine protease. Our results suggest that class XI plant myosin requires TCP-1alpha for regulating folding or providing protection against denaturation.
authors.affiliation: Biology Department, University of Louisiana, Lafayette 70504, USA.
authors.forename: Zhengyuan
authors.initials: Z
authors.lastname: Wang
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Pesacreta
mesh_terms: D000199:Actins / Q000032:analysis; D015153:Blotting, Western; D002374:Catalase / Q000032:analysis; D002467:Cell Nucleus / Q000737:chemistry; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins / Q000032:analysis* / Q000378:metabolism; D002736:Chloroplasts / Q000737:chemistry; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D018548:Cotyledon / Q000737:chemistry / Q000166:cytology; D004721:Endoplasmic Reticulum / Q000737:chemistry; D006056:Golgi Apparatus / Q000737:chemistry; D050883:HSC70 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis; D018519:Meristem / Q000737:chemistry / Q000166:cytology; D008856:Microscopy, Fluorescence; D008928:Mitochondria / Q000737:chemistry*; D009218:Myosins / Q000032:analysis* / Q000145:classification / Q000378:metabolism; D020675:Peroxisomes / Q000737:chemistry; D019441:Plant Epidermis / Q000737:chemistry / Q000166:cytology; D018515:Plant Leaves / Q000737:chemistry / Q000166:cytology; D010940:Plant Proteins / Q000032:analysis / Q000378:metabolism; D018517:Plant Roots / Q000737:chemistry / Q000254:growth & development; D018087:Plastids / Q000737:chemistry*; D018272:Porins / Q000032:analysis; D011485:Protein Binding; D020033:Protein Isoforms / Q000032:analysis / Q000145:classification / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000737:chemistry; D013347:Subcellular Fractions / Q000737:chemistry; D003313:Zea mays / Q000737:chemistry*
chemical_list: D000199:Actins; D050883:HSC70 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D010940:Plant Proteins; D018272:Porins; D020033:Protein Isoforms; D015842:Serine Proteinase Inhibitors; C089962:por1 protein, Zea mays; D002374:Catalase; D056404:Chaperonin Containing TCP-1; D018833:Chaperonins; D009218:Myosins