Partial sequencing and mapping of clones from two maize cDNA libraries

Shen, Ben; Carneiro, N. P.; Torres‐Jerez, Ivone; Stevenson, Becky; McCreery, Thomas P.; Helentjaris, Tim; Baysdorfer, Chris; Almira, Ernesto C.; Ferl, Robert J.; Habben, Jeffrey E.

doi:10.1007/bf00040691

Cited by 86 publications

(46 citation statements)

References 28 publications

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“…The full cDNA insert from clone 5C06B09 (Shen et al, 1994) is 830 nucleotides long and contains a major open reading frame of 396 nucleotides, a consensus translation start site, and a poly(A) tail of 35 nucleotides. The 5 Ј and 3 Ј untranslated regions are 115 and 285 nucleotides, respectively.…”

Section: Zmpro4 Encodes a Plant Profilinmentioning

confidence: 99%

Pollen Profilin Function Depends on Interaction with Proline-Rich Motifs

et al. 1998

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The actin binding protein profilin has dramatic effects on actin polymerization in vitro and in living cells. Plants have large multigene families encoding profilins, and many cells or tissues can express multiple profilin isoforms. Recently, we characterized several profilin isoforms from maize pollen for their ability to alter cytoarchitecture when microinjected into living plant cells and for their association with poly-L -proline and monomeric actin from maize pollen. In this study, we characterize a new profilin isoform from maize, which has been designated ZmPRO4, that is expressed predominantly in endosperm but is also found at low levels in all tissues examined, including mature and germinated pollen. The affinity of ZmPRO4 for monomeric actin, which was measured by two independent methods, is similar to that of the three profilin isoforms previously identified in pollen. In contrast, the affinity of ZmPRO4 for poly-L -proline is nearly twofold higher than that of native pollen profilin and the other recombinant profilin isoforms. When ZmPRO4 was microinjected into plant cells, the effect on actin-dependent nuclear position was significantly more rapid than that of another pollen profilin isoform, ZmPRO1. A gain-of-function mutant (ZmPRO1-Y6F) was created and found to enhance poly-L -proline binding activity and to disrupt cytoarchitecture as effectively as ZmPRO4. In this study, we demonstrate that profilin isoforms expressed in a single cell can have different effects on actin in living cells and that the poly-L -proline binding function of profilin may have important consequences for the regulation of actin cytoskeletal dynamics in plant cells. INTRODUCTIONThe male gametes of plants are delivered to the ovule by a unique mode of motility that is dependent on cellular morphogenesis of the pollen grain (reviewed in Bedinger and Edgerton, 1989;Mascarenhas, 1993;Taylor and Hepler, 1997). Mature pollen is a haploid multicellular structure consisting of a large vegetative cell and one generative cell or two sperm cells. The sperm are derived from a mitotic division of the generative cell that occurs before pollen maturation or during pollen tube extension. When a pollen grain lands on a receptive stigma, the vegetative cell forms a tipgrowing protuberance, the pollen tube, that extends down the transmitting tissue of the style toward the ovule. Remarkably, the growth rate of the maize pollen tube can exceed 1 cm/hr (Bedinger, 1992). The pollen tube delivers the sperm cells to the embryo sac, where they are deposited to fuse with the egg cell and central cell.Both pollen germination and pollen tube elongation are dependent on the actin cytoskeleton, as determined through studies with cytochalasins (reviewed in Pierson and Cresti, 1992;Taylor and Hepler, 1997). The actin cytoskeleton in pollen is highly dynamic, and dramatic rearrangements occur during pollen germination. Actin microfilaments focus on the germination aperture(s) before generation of the pollen tube and become arranged in long axial bundles t...

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Section: Zmpro4 Encodes a Plant Profilinmentioning

confidence: 99%

Pollen Profilin Function Depends on Interaction with Proline-Rich Motifs

et al. 1998

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“…An eEFlA cDNA fragment corresponding to the carboxyl domain of the protein (Shen et al, 1994) was labeled with digoxigenin and used to screen a maize endosperm cDNA library (Habben et al, 1993). Plaque lifting and membrane treatment were performed as described previously (Shen et al, 1994).…”

Section: Lsolation and Characterization Of Eefl A C D N A Clonesmentioning

confidence: 99%

“…Plaque lifting and membrane treatment were performed as described previously (Shen et al, 1994). Filter hybridization and washing were done according to McCreery and Helentjaris (1994).…”

Section: Lsolation and Characterization Of Eefl A C D N A Clonesmentioning

confidence: 99%

“…As shown in Figure 3A Once eEFIA was purified to homogeneity, we compared the amino acid sequence with that encoded by an endosperm mRNA. A partial eEFIA cDNA clone of 1.2 kb has been isolated from a maize endosperm cDNA library (Shen et al, 1994), and we used this clone as a probe to isolate a full-length cDNA. eEF!AZME16 was found to have an identical nucleotide sequence to that of the probe.…”

Section: Accumulation Of Eefia During Endosperm Developmentmentioning

confidence: 99%

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Characterization of Maize Elongation Factor 1A and Its Relationship to Protein Quality in the Endosperm

et al. 1997

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The protein synthesis elongation factor I A (eEF1 A) is a multifunctional protein in eukaryotic cells. In maize (Zea mays 1.) endosperm eEFlA co-localizes with actin around protein bodies, and its accumulation is highly correlated with the protein-bound lysine (Lys) content. We purified eEFlA from maize kernels by ammonium sulfate precipitation, ion-exchange, and chromatofocusing. The identity of the purified protein was confirmed by microsequencing of an endoproteinase glutamic acid-C fragment and by its ability to bundle actin. Using purified eEFlA as a standard, we found that this protein contributes 0.4% of the total protein in W64A+ endosperm and approximately 1 O/O of the protein in W64Ao2. Because eEFlA contains 10% Lys, it accounts for 2.2% of the total Lys in W64A+ and 2.3% of the Lys in W64Ao2. However, its concentration predicts 90% of the Lys found in endosperm proteins of both genotypes, indicating that eEFlA is a key component of the group of proteins that determines the nutritional quality of the grain. This notion is further supported by the fact that in froury2, another high-lys mutant, the content of eEFlA increases with the dosage of the f/oury2 gene. These data provide the biochemical basis for further investigation of the relationship between eEFl A content and the nutritional quality of cereals.

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“…ESTs help to quickly identify functions of expressed genes and to understand the complexity of gene expression. ESTs have also served as molecular genetic markers in genomic mapping (Kurata et al, 1994;Shen et al, 1994). Since the number of ESTs from various species has increased rapidly, it is now possible to compare a large number of genes and the proteins they encode between animals and plants.…”

mentioning

confidence: 99%

Expressed Sequence Tags of Chinese Cabbage Flower Bud cDNA

Lim

Kim

et al. 1996

Plant Physiology

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We randomly selected and partially sequenced cDNA clones from a library of Chinese cabbage (Brassica campestris L. ssp. pekinensis) flower bud cDNAs. Out of 1216 expressed sequence tags (ESTs), 904 cDNA clones were unique or nonredundant. Five hundred eighty-eight clones (48.4%) had sequence homology to functionally defined genes at the peptide level. Only 5 clones encoded known flower-specific proteins. Among the cDNAs with no similarity to known protein sequences (628), 184 clones had significant similarity to nucleotide sequences registered in the databases. Among these 184 clones, 142 exhibited similarities at the nucleotide level only with plant ESTs. Also, sequence similarities were evident between these 142 ESTs and their matching ESTs when compared using the deduced amino acid sequences. Therefore, it is possible that the anonymous ESTs encode plant-specific ubiquitous proteins. Our extensive EST analysis of genes expressed in floral organs not only contributes to the understanding of the dynamics of genome expression patterns in floral organs but also adds data to the repertoire of all genomic genes.

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Partial sequencing and mapping of clones from two maize cDNA libraries

Cited by 86 publications

References 28 publications

Pollen Profilin Function Depends on Interaction with Proline-Rich Motifs

Pollen Profilin Function Depends on Interaction with Proline-Rich Motifs

Characterization of Maize Elongation Factor 1A and Its Relationship to Protein Quality in the Endosperm

Expressed Sequence Tags of Chinese Cabbage Flower Bud cDNA

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