matching names were searched using amino acid sequences retrieved in the annotated tomato genome database ( Bombarely et al., 2011 ). For proteins assigned to multiple accessions in A. thaliana , the one annotated to salt or relevant stress factors and
Peter Nveawiah-Yoho, Jing Zhou, Marsha Palmer, Roger Sauve, Suping Zhou, Kevin J. Howe, Tara Fish and Theodore W. Thannhauser
Paweł Wójcik, Anna Skorupińska and Hamide Gubbuk
-containing preparations (classified by the European Union as growth regulators) are also critical factors limiting their use in plant production. To overcome the problems related to use of auxins, application of the amino acid L-TRP, a precursor of IAA ( Pattison et al
Hai-nan Liu, Jian-rong Feng, Xiao-fang Liu, Wen-hui Li, Wen-juan Lv and Ming Luo
sequencing ( Fig. 2B ). The deduced amino acid sequence of the fragment contained an F-box domain, V1, V2, HVa, and HVb. The structural characteristics were similar to SFB in other Rosaceae species. The deduced amino acid sequence had 91% identity with the
Robert A. Saftner
The ethylene precursor, 1 -aminocyclopropane- 1 -carboxylic acid (ACC), is actively transported across the tonoplast of plant cells, impacting cellular compartmentation of ACC and ethylene biosynthesis. To identify potential photoaffinity probes for identifying ACC transport-related membrane proteins, the effects of over 70 ACC and other amino acid analogs on ACC uptake into isolated maize vacuoles were investigated. Only relatively nonpolar, neutral amino acid stereoisomers of L-configuration were strong inhibitors of ACC transport. Group additions, substitutions, or deletions at the carboxyl, (x-amino and the Pro-(R) methylene, or hydrogen moieties essentially eliminated transport inhibition, whereas side-chain substitutions remained antagonistic. The kinetics of ACC and neutral L-amino acid analogs tested were competitive. The results indicate that the ACC transport system can be classified as a neutral L-amino acid carrier having a relatively high affinity for ACC and other nonpolar amino acids. The results also suggest that the carrier interacts with the carboxyl, alpha-amino, and Pro-(R) groups and the side chain of substrate amino acids. Based on these findings, potential photoaffinity probes of the ACC transport system have been identified.
Jing Ma, Zheng Li, Bin Wang, Shunzhao Sui and Mingyang Li
CpEXP1 (GeneBank accession number: JN700522), encoded a putative protein of 257 amino acids with a molecular mass of 27.7 kDa and an isoelectric point of 7.8. The common features of the α-expansin subfamily such as eight conserved cysteine residues
Shutian Tao, Danyang Wang, Cong Jin, Wei Sun, Xing Liu, Shaoling Zhang, Fuyong Gao and Shahrokh Khanizadeh
(BLAST) web page ( Beck et al., 2013 ). Deduced amino acid sequences were obtained with the Primer 5.0 software program (Premier Biosoft, Palo Alto, CA). Phylogenetic relationships among sequences were determined with the MEGA 6.06 software program (MEGA
Suping Zhou, Marsha Palmer, Jing Zhou, Sarabjit Bhatti, Kevin J. Howe, Tara Fish and Theodore W. Thannhauser
, stress proteins; Group 2, gene expression; Group 3, nascent protein processing and protein folding; Group 4, protein degradation; Group 5, carbohydrate metabolism; Group 6, amino acid and nucleotide metabolism; Group 7, lipid metabolism; Group 8, ATPases
Zhongchun Jiang, Chenping Xu and Bingru Huang
induces leaf senescence ( Lim et al., 2007 ). In senescing leaves, N catabolism occurs and proteins are degraded to produce NH 3 and amino acids, which are used to produce glutamine (Gln) for N transport to young leaves and other sink organs for reuse
Zhou Li, Yan Peng and Bingru Huang
recent years, a nonprotein amino acid, GABA, has been found to exhibit PGR effects due to its central roles in maintaining carbon and nitrogen balance and its involvement in carbohydrate and amino acid metabolism ( Barbosa et al., 2010 ; Bouché and Fromm
Lawford Baxter and Luther Waters Jr.
Okra (Abelmoschus esculentus L. Moench) pods stored In a controlled atmosphere (CA) of 5% O2 and 10% CO2 at 11 ± 1C and in air at the same temperature (RA) were compared to determine the effects of the two storage environments on changes in sugars, organic acids, proteins and amino acids, and ascorbic acid contents within the tissue. Pods were sampled at 3-day intervals for 12 days. CA-stored pods generally had greater retention of sugars, soluble proteins, and amino acids than RA-stored pods. Citric, malic, and ascorbic acids contents of CA pods also declined more slowly than those of RA pods.