scholarly journals Amino acid sequence similarity between GCN3 and GCD2, positive and negative translational regulators of GCN4: evidence for antagonism by competition.

Genetics ◽  
1989 ◽  
Vol 122 (3) ◽  
pp. 551-559 ◽  
Author(s):  
C J Paddon ◽  
E M Hannig ◽  
A G Hinnebusch
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
Normal Growth ◽  
Growth Conditions ◽  
Amino Acid Sequence Similarity ◽  
Predicted Amino Acid Sequence ◽  
Carboxyl Terminal ◽  
Translational Regulators ◽  
Starvation Conditions

Abstract The GCD2 gene product is required in conditions of amino acid sufficiency to repress the synthesis of GCN4, a transcriptional activator of amino acid biosynthetic genes in Saccharomyces cerevisiae. GCD2 is also required unconditionally for cell viability. The constitutive derepression of GCN4 expression and temperature sensitivity for growth associated with GCD2 alleles, known as gcd12 mutations, are completely masked by wild-type GCN3, a positive regulator of GCN4 expression. This observation suggests that GCN3 can promote or at least partially substitute for GCD2 function in normal growth conditions, while acting as an antagonist of GCD2 in amino acid starvation conditions. We report here that the predicted amino acid sequence of GCN3 shows extensive similarity with the carboxyl-terminal portion of GCD2. Based on this finding, it seems likely that gcd12 mutations specifically affect the domain of GCD2 that is similar in sequence to GCN3. We propose that GCN3 can substitute for this domain in a gcd12 mutant grown in normal growth conditions, and that modification of GCN3 in starvation conditions causes it to interfere with, rather than substitute for GCD2 function. A gcd2 deletion and gcd2-1 are each expected to inactivate a second domain for which GCN3 cannot substitute, accounting for the inability of GCN3 to mask the phenotypes associated with these mutations.

scholarly journals Isolation and Functional Analysis of CmMAX1 from Chrysanthemum

2018 ◽  
Vol 143 (6) ◽  
pp. 430-435
Author(s):  
Lili Dong ◽  
Qi Wang ◽  
Feng Xiong ◽  
Na Liu ◽  
ShuiMing Zhang
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
Regulatory Gene ◽  
Chrysanthemum Morifolium ◽  
Amino Acid Sequence Similarity ◽  
Predicted Amino Acid Sequence ◽  
Binding Motif ◽  
P Deficiency ◽  
Significant Difference

More axillary buds 1 (MAX1), initially identified in arabidopsis (Arabidopsis thaliana), is a key regulatory gene in strigolactone synthesis. CmMAX1, an ortholog of MAX1 was cloned from chrysanthemum (Chrysanthemum morifolium cv. Jinba). It had an open reading frame of 1611 bp and encoded 536 amino acid of P450 protein, with a conserved heme-binding motif of PFG × GPR × C × G, as well as PERF and KExxR motifs. The predicted amino acid sequence of CmMAX1 was most closely related to the MAX1 ortholog identified in lotus (Nelumbo nucifera), NnMAX1, with 55.33% amino acid sequence similarity. Expression analysis revealed there was no significant difference of CmMAX1 expression among various tissues. Phosphorus (P) deficiency significantly improved the expression levels of CmMAX1. Strigolactone, auxin, and cytokinin negatively regulated the expression of CmMAX1. Overexpression of CmMAX1 reduced the branch numbers of arabidopsis max1-1. These results suggest that CmMAX1 may be a candidate gene for reducing the shoot branching of chrysanthemum.

Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function

1988 ◽  
Vol 8 (11) ◽  
pp. 4808-4820
Author(s):  
E M Hannig ◽  
A G Hinnebusch
Keyword(s):  
Amino Acid ◽  
Normal Growth ◽  
Growth Conditions ◽  
Regulatory Function ◽  
Regulatory Sequences ◽  
Noncoding Dna ◽  
Physical Description ◽  
Amino Acid Availability ◽  
Translational Activator ◽  
Starvation Conditions

GCN4 encodes a transcriptional activator of amino acid biosynthetic genes in Saccharomyces cerevisiae. The GCN3 product is a positive regulator required for increased synthesis of GCN4 protein in amino acid-starved cells. GCN3 appears to act indirectly by antagonizing GCD-encoded negative regulators of GCN4 expression under starvation conditions; however, GCN3 can also suppress the effects of gcd12 mutations under nonstarvation conditions. These results imply that the GCN3 product can promote either repression or activation of GCN4 expression depending on amino acid availability. We present a complete physical description of the GCN3 gene and its transcript, plus measurements of GCN3 expression at the transcriptional and translational levels under different growth conditions. GCN3 encodes a 305-amino-acid polypeptide with no significant homology to any other known protein sequence. GCN3 mRNA contains no leader AUG codons, and no potential GCN4 binding sites were found in GCN3 5' noncoding DNA. In accord with the absence of these regulatory sequences found at other genes in the general control system, GCN3 mRNA and a GCN3-lacZ fusion enzyme are present at similar levels under both starvation and nonstarvation conditions. These data suggest that modulation of GCN3 regulatory function in response to amino acid availability occurs posttranslationally. A gcn3 deletion leads to unconditional lethality in a gcd1-101 mutant, supporting the idea that GCN3 is expressed under normal growth conditions and cooperates with the GCD1 product under these circumstances to carry out an essential cellular function. We describe a point mutation that adds three amino acids to the carboxyl terminus of GCN3, which inactivates its positive regulatory function required under starvation conditions without impairing its ability to promote functions carried out by GCD12 under nonstarvation conditions.

scholarly journals Engineered Resistance Against Papaya ringspot virus in Venezuelan Transgenic Papayas

Plant Disease ◽  
2004 ◽  
Vol 88 (5) ◽  
pp. 516-522 ◽  
Author(s):  
Gustavo Fermin ◽  
Valentina Inglessis ◽  
Cesar Garboza ◽  
Sairo Rangel ◽  
Manuel Dagert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Agrobacterium Tumefaciens ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
Ringspot Virus ◽  
Amino Acid Sequence Similarity ◽  
Papaya Ringspot Virus ◽  
Local Varieties ◽  
Cp Gene

Local varieties of papaya grown in the Andean foothills of Mérida, Venezuela, were transformed independently with the coat protein (CP) gene from two different geographical Papaya ringspot virus (PRSV) isolates, designated VE and LA, via Agrobacterium tumefaciens. The CP genes of both PRSV isolates show 92 and 96% nucleotide and amino acid sequence similarity, respectively. Four PRSV-resistant R0 plants were intercrossed or selfed, and the progenies were tested for resistance against the homologous isolates VE and LA, and the heterologous isolates HA (Hawaii) and TH (Thailand) in greenhouse conditions. Resistance was affected by sequence similarity between the transgenes and the challenge viruses: resistance values were higher for plants challenged with the homologous isolates (92 to 100% similarity) than with the Hawaiian (94% similarity) and, lastly, Thailand isolates (88 to 89% similarity). Our results show that PRSV CP gene effectively protects local varieties of papaya against homologous and heterologous isolates of PRSV.

scholarly journals Identification and Characterization of a NaCl-Responsive Genetic Locus Involved in Survival during Desiccation in Sinorhizobium meliloti

2013 ◽  
Vol 79 (18) ◽  
pp. 5693-5700 ◽  
Author(s):  
Jan A. C. Vriezen ◽  
Frans J. de Bruijn ◽  
Klaus Nüsslein
Keyword(s):  
Sinorhizobium Meliloti ◽  
Agricultural Soils ◽  
Sequence Similarity ◽  
Genetic Locus ◽  
Model Organism ◽  
Normal Growth ◽  
Growth Conditions ◽  
Amino Acid Sequence Similarity ◽  
Content Type ◽  
Genetic Mechanisms

ABSTRACTTheRhizobiaceaeare a bacterial family of enormous agricultural importance due to the ability of its members to fix atmospheric nitrogen in an intimate relationship with plants. Their survival as naturally occurring soil bacteria in agricultural soils as well as popular seed inocula is affected directly by drought and salinity. Survival after desiccation in the presence of NaCl is enabled by underlying genetic mechanisms in the model organismSinorhizobium meliloti1021. Since salt stress parallels a loss in water activity, the identification of NaCl-responsive loci may identify loci involved in survival during desiccation. This approach enabled identification of the lociasnOandnggby their reduced ability to grow on increased NaCl concentrations, likely due to their inability to produce the osmoprotectant N-acetylglutaminylglutamine (NAGGN). In addition, the mutant harboringngg::Tn5luxABwas affected in its ability to survive desiccation and responded to osmotic stress. The desiccation sensitivity may have been due to secondary functions of Ngg (N-acetylglutaminylglutamine synthetase)-like cell wall metabolism as suggested by the presence of ad-alanine-d-alanine ligase (dAla-dAla) domain and by sensitivity of the mutant to β-lactam antibiotics.asnO::Tn5luxABis expressed during the stationary phase under normal growth conditions. Amino acid sequence similarity to enzymes producing β-lactam inhibitors and increased resistance to β-lactam antibiotics may indicate thatasnOis involved in the production of a β-lactam inhibitor.

scholarly journals High-Efficiency Utilization of the Bovine Integrin αvβ3 as a Receptor for Foot-and-Mouth Disease Virus Is Dependent on the Bovine β3Subunit

2000 ◽  
Vol 74 (16) ◽  
pp. 7298-7306 ◽  
Author(s):  
Sherry Neff ◽  
Peter W. Mason ◽  
Barry Baxt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Disease Virus ◽  
Sequence Similarity ◽  
Foot And Mouth Disease ◽  
Viral Proteins ◽  
Mouth Disease ◽  
Amino Acid Sequence Similarity ◽  
Mouth Disease Virus ◽  
Human Integrin

ABSTRACT We have previously reported that Foot-and-mouth disease virus (FMDV), which is virulent for cattle and swine, can utilize the integrin αvβ3 as a receptor on cultured cells. Since those studies were performed with the human integrin, we have molecularly cloned the bovine homolog of the integrin αvβ3 and have compared the two receptors for utilization by FMDV. Both the αv and β3subunits of the bovine integrin have high degrees of amino acid sequence similarity to their corresponding human subunits in the ectodomains (96%) and essentially identical transmembrane and cytoplasmic domains. Within the putative ligand-binding domains, the bovine and human αv subunits have a 98.8% amino acid sequence similarity while there is only a 93% similarity between the β3 subunits of these two species. COS cell cultures, which are not susceptible to FMDV infection, become susceptible if cotransfected with αv and β3 subunit cDNAs from a bovine or human source. Cultures cotransfected with the bovine αvβ3 subunit cDNAs and infected with FMDV synthesize greater amounts of viral proteins than do infected cultures cotransfected with the human integrin subunits. Cells cotransfected with a bovine αv subunit and a human β3subunit synthesize viral proteins at levels equivalent to those in cells expressing both human subunits. However, cells cotransfected with the human αv and the bovine β3 subunits synthesize amounts of viral proteins equivalent to those in cells expressing both bovine subunits, indicating that the bovine β3 subunit is responsible for the increased effectiveness of this receptor. By engineering chimeric bovine-human β3subunits, we have shown that this increase in receptor efficiency is due to sequences encoding the C-terminal one-third of the subunit ectodomain, which contains a highly structured cysteine-rich repeat region. We postulate that amino acid sequence differences within this region may be responsible for structural differences between the human and bovine β3 subunit, leading to more efficient utilization of the bovine receptor by this bovine pathogen.

Sign in / Sign up

Export Citation Format

Share Document