title: Maize profilin isoforms are functionally distinct.
abstract: Profilin is an actin monomer binding protein that, depending on the conditions, causes either polymerization or depolymerization of actin filaments. In plants, profilins are encoded by multigene families. In this study, an analysis of native and recombinant proteins from maize demonstrates the existence of two classes of functionally distinct profilin isoforms. Class II profilins, including native endosperm profilin and a new recombinant protein, ZmPRO5, have biochemical properties that differ from those of class I profilins. Class II profilins had higher affinity for poly-l-proline and sequestered more monomeric actin than did class I profilins. Conversely, a class I profilin inhibited hydrolysis of membrane phosphatidylinositol-4,5-bisphosphate by phospholipase C more strongly than did a class II profilin. These biochemical properties correlated with the ability of class II profilins to disrupt actin cytoplasmic architecture in live cells more rapidly than did class I profilins. The actin-sequestering activity of both maize profilin classes was found to be dependent on the concentration of free calcium. We propose a model in which profilin alters cellular concentrations of actin polymers in response to fluctuations in cytosolic calcium concentration. These results provide strong evidence that the maize profilin gene family consists of at least two classes, with distinct biochemical and live-cell properties, implying that the maize profilin isoforms perform distinct functions in the plant.
authors.affiliation: Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.
authors.forename: D R
authors.initials: DR
authors.lastname: Kovar
authors.forename: B K
authors.initials: BK
authors.lastname: Drøbak
authors.forename: C J
authors.initials: CJ
authors.lastname: Staiger
mesh_terms: D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D002118:Calcium / Q000378:metabolism / Q000494:pharmacology; D003001:Cloning, Molecular; D003285:Contractile Proteins; D003593:Cytoplasm / Q000187:drug effects / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis / Q000187:drug effects; D008840:Microfilament Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000378:metabolism; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011058:Pollen / Q000737:chemistry / Q000166:cytology / Q000235:genetics / Q000378:metabolism; D051304:Profilins; D011485:Protein Binding / Q000187:drug effects; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D012639:Seeds / Q000737:chemistry / Q000166:cytology / Q000235:genetics / Q000378:metabolism; D010738:Type C Phospholipases / Q000037:antagonists & inhibitors / Q000378:metabolism; D003313:Zea mays / Q000737:chemistry / Q000166:cytology / Q000235:genetics / Q000378:metabolism
chemical_list: D000199:Actins; D003285:Contractile Proteins; D008840:Microfilament Proteins; D010455:Peptides; D019269:Phosphatidylinositol 4,5-Diphosphate; D010940:Plant Proteins; D051304:Profilins; D020033:Protein Isoforms; D012333:RNA, Messenger; D011994:Recombinant Proteins; C011083:polyproline; D000255:Adenosine Triphosphate; D010738:Type C Phospholipases; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D002118:Calcium