Identification of differentially expressed genes during early development of tomato fruit. Characterisation of a novel cDNA coding for a RAD23 protein.

2000 ◽  
Vol 27 (10) ◽  
pp. 911
Author(s):  
Martine Lemaire-Chamley ◽  
Johann Petit ◽  
Mathilde Causse ◽  
Philippe Raymond ◽  
Christian Chevalier

Before the onset of ripening, tomato fruit development comprises three distinct phases: fruit set, a cell division phase and a cell expansion phase. In this study, we used the method of mRNA differential display in order to isolate tomato genes specifically expressed during these early phases of fruit development. Among 40 differen-tial bands, nine cDNAs were selected for further investigations based on their identification after nucleotide sequencing. We isolated the full-length cDNA corresponding to one of these fragments, coding for RAD23, a protein involved in the excision repair system, thus providing new sequence information on a poorly characterised protein in plants. All the isolated cDNAs were mapped on the tomato genome and their expression studied by northern blot and semi-quantitative RT–PCR during early fruit development and in vegetative organs of tomato plants. The sequence data are deposited in the GenBank under the accession numbers: AJ270956 (mo5-3C11/1), AJ270957 (mo5-3G12/4), AJ270958 (mo5-3G17), AJ270959 (mo5-3T12), AJ270960 (mo1-6A1), AJ270961 (mo1-6T1), AJ270962 (mo5-10G1), AJ270963 (mo6-20G1), AJ270964 (mo6-MGT2) and AJ243875 (LeRAD23-8 full-length cDNA).

1999 ◽  
Vol 345 (1) ◽  
pp. 43-52 ◽  
Author(s):  
Angélique AUGUSTIN ◽  
Hélène MULLER-STEFFNER ◽  
Francis SCHUBER

Bovine spleen ecto-NAD+ glycohydrolase, an archetypal member of the mammalian membrane-associated NAD(P)+ glycohydrolase enzyme family (EC 3.2.2.6), displays catalytic features similar to those of CD38, i.e. a protein originally described as a lymphocyte differentiation marker involved in the metabolism of cyclic ADP-ribose and signal transduction. Using amino acid sequence information obtained from NAD+ glycohydrolase and from a truncated and hydrosoluble form of the enzyme (hNADase) purified to homogeneity, a full-length cDNA clone was obtained. The deduced sequence indicates a protein of 278 residues with a molecular mass of 31.5 kDa. It predicts that bovine ecto-NAD+ glycohydrolase is a type II transmembrane protein, with a very short intracellular tail. The bulk of the enzyme, which is extracellular and contains two potential N-glycosylation sites, yields the fully catalytically active hNADase which is truncated by 71 residues. Transfection of HeLa cells with the full-length cDNA resulted in the expression of the expected NAD+ glycohydrolase, ADP-ribosyl cyclase and GDP-ribosyl cyclase activities at the surface of the cells. The bovine enzyme, which is the first ‘classical’ NAD(P)+ glycohydrolase whose structure has been established, presents a particularly high sequence identity with CD38, including the presence of 10 strictly conserved cysteine residues in the ectodomain and putative catalytic residues. However, it lacks two otherwise conserved cysteine residues near its C-terminus. Thus hNADase, the truncated protein of 207 amino acids, represents the smallest functional domain endowed with all the catalytic activities of CD38/NAD+ glycohydrolases so far identified. Altogether, our data strongly suggest that the cloned bovine spleen ecto-NAD+ glycohydrolase is the bovine equivalent of CD38.


1988 ◽  
Vol 253 (3) ◽  
pp. 919-922 ◽  
Author(s):  
G Tromp ◽  
H Kuivaniemi ◽  
A Stacey ◽  
H Shikata ◽  
C T Baldwin ◽  
...  

A full-length cDNA clone for the human prepro alpha 1(I) chain of type I procollagen was characterized. Nucleotide sequencing of the first 1500 nucleotide residues of the 5′-end of the cDNA clone provided 729 nucleotide residues and the codons for 243 amino acid residues not previously defined from any species. The data made it possible, for the first time, to compare completely codon usage for the human alpha 1(I) and alpha 2(I) chains.


2001 ◽  
Vol 11 (2) ◽  
pp. 281-289
Author(s):  
Hideaki Konno ◽  
Yoshifumi Fukunishi ◽  
Kazuhiro Shibata ◽  
Masayoshi Itoh ◽  
Piero Carninci ◽  
...  

We developed computer-based methods for constructing a nonredundant mouse full-length cDNA library. Our cDNA library construction process comprises assessment of library quality, sequencing the 3′ ends of inserts and clustering, and completing a re-array to generate a nonredundant library from a redundant one. After the cDNA libraries are generated, we sequence the 5′ ends of the inserts to check the quality of the library; then we determine the sequencing priority of each library. Selected libraries undergo large-scale sequencing of the 3′ ends of the inserts and clustering of the tag sequences. After clustering, the nonredundant library is constructed from the original libraries, which have redundant clones. All libraries, plates, clones, sequences, and clusters are uniquely identified, and all information is saved in the database according to this identifier. At press time, our system has been in place for the past two years; we have clustered 939,725 3′ end sequences into 127,385 groups from 227 cDNA libraries/sublibraries (seehttp://genome.gse.riken.go.jp/).[The sequence data described in this paper have been submitted to the DDBJ data library under accession nos. AV00011–AV175734, AV204013–AV382295, andBB561685–BB609425.]


2009 ◽  
Vol 35 (4) ◽  
pp. 602-607 ◽  
Author(s):  
Dong WU ◽  
Jun-Jie LIU ◽  
Shu-Xun YU ◽  
Shu-Li FAN ◽  
Mei-Zhen SONG

2013 ◽  
Vol 20 (4) ◽  
pp. 722-732
Author(s):  
Bing LI ◽  
Jie WANG ◽  
Chengfeng ZHANG ◽  
Jian ZHU

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