0.096453957 The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
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Abstract of related literatures
1. Pi-class glutathione S-transferases (GSTs) play an important role in the detoxification of chemical toxins and mutagens and are implicated in neoplastic development and drug resistance. In all species characterized to date, only one functional Pi-class GST gene has been described. In this report we have identified two actively transcribed murine Pi-class GST genes, Gst p-1 and Gst p-2. The coding regions of Gst p-1 and the mouse Pi-class GST cDNA (GST-II) reported by Hatayama, Satoh and Satoh (1990) (Nucleic Acids Res. 18, 4606) are identical, whereas Gst p-2 encodes a protein that has not been described previously. The two genes are approximately 3 kb long and contain seven exons interrupted by six introns. In addition to a TATA box and a sequence motif matching the phorbol-ester-responsive element, the promoters of Gst p-1 and Gst p-2 exhibit one and two G+C boxes (GGGCGG) respectively. The cDNAs of the two genes were isolated from total liver RNA using reverse PCR. The peptide sequence deduced from the cDNAs share 97% identity and differ in six amino acids. Both genes are transcribed at significantly higher levels in male mouse liver than in female, and Gst p-1 mRNA is more abundant in both sexes than Gst p-2. PMID: [8135745]
2. An 8-kilobase mouse genomic fragment containing two intact glutathione S-transferase (GST) genes has been isolated from a mouse lambda genomic library. Each of the genes (designated mGSTpiA and mGSTpiB) is less than 3 kilobases in size and is comprised of seven exons that give rise to a 630-base pair open reading frame encoding 209 amino acids. The deduced amino acid sequences of the gene products differ in only 6 amino acids at positions 10, 11, 89, 104, 106, and 109. These two genes are highly homologous to rat GST-P and to a lesser extent to human GST-pi. Northern blot analysis of mRNAs from a variety of mouse tissues demonstrated that mGSTpiB is ubiquitously expressed, whereas mGST-piA is more selectively expressed in gallbladder, colon, heart, and skeletal muscle. Primer extension analysis revealed four potential transcription start sites in mGST-piB and one in mGSTpiA. Although both genes were expressed in vitro and in vivo only mGSTpiB product metabolized 1-chloro-2,4-dinitrobenzene, a common GST substrate. Further in vitro expression studies of three chimeric mGSTpi genes suggested that one or both of the amino acids at positions 10 and 11 of mouse GSTpi enzymes are important for the enzyme's ability to metabolize 1-chloro-2,4-dinitrobenzene. PMID: [7982937]
3. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334]
Conjugation of reduced glutathione to a wide number ofexogenous and endogenous hydrophobic electrophiles. Cannotmetabolize 1-chloro-2,4-dinitrobenzene.