Biomaterial Database

The structure and organization of a proline-rich protein gene of a mouse multigene family. 1985

D K Ann, and D M Carlson

One gene of the mouse proline-rich protein multigene family was cloned on a 3.6-kilobase pair EcoRI/BglII DNA fragment from a (partial) Sau3A bacteriophage library of CD-1 mouse chromosomal DNA. Phage harboring the gene were identified by plaque hybridization using 32P-labeled proline-rich protein cDNA inserts from clones pRP33 and pMP1 obtained from rat and mouse, respectively. The transcriptional unit includes three exonic sequences separated by 1434 base pairs (intron I) and 450 base pairs (intron II). The complete primary structure of the gene and the 5' and 3' flanking regions (3595 base pairs) were determined by the Maxam and Gilbert (Maxam, A.M., and Gilbert, W. (1980) Methods Enzymol. 65, 499-560) sequencing method. The DNA on the 5' side of exon I contains several sequences that may be involved in the induction and expression of this mouse gene. These sequences include putative regulatory sites such as those considered to be inducible by cAMP and steroids, Z-DNA and enhancer sequences and the expected TATAA and CAAT boxes. The mature protein coding region, exon II, is not interrupted with intron sequences. Exon III is located in the nontranslated region and contains the poly(A) addition site. The deduced amino acid sequence showed that the protein encoded by this gene contains 13 tandemly repeat regions, each 14 amino acids in length, with the prototype sequence PPPPGGPQPRPPQG. Each amino acid within the repeat has a favored codon. The consensus DNA sequence for each repeat is CCA CCA CCA CCA GGA GGC CCA CAG CCG AGA CCC CCT CAA GGC. The high degree of conservation of both nucleotide and amino acid sequences within the repeat region suggests that proline-rich protein genes likely evolved by gene duplication of a 42-base pair internal repeat.

UI	MeSH Term	Description	Entries
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D009693	Nucleic Acid Hybridization	Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503)	Genomic Hybridization,Acid Hybridization, Nucleic,Acid Hybridizations, Nucleic,Genomic Hybridizations,Hybridization, Genomic,Hybridization, Nucleic Acid,Hybridizations, Genomic,Hybridizations, Nucleic Acid,Nucleic Acid Hybridizations
D010455	Peptides	Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS.	Peptide,Polypeptide,Polypeptides
D004247	DNA	A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).	DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004262	DNA Restriction Enzymes	Enzymes that are part of the restriction-modification systems. They catalyze the endonucleolytic cleavage of DNA sequences which lack the species-specific methylation pattern in the host cell's DNA. Cleavage yields random or specific double-stranded fragments with terminal 5'-phosphates. The function of restriction enzymes is to destroy any foreign DNA that invades the host cell. Most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. They are also used as tools for the systematic dissection and mapping of chromosomes, in the determination of base sequences of DNAs, and have made it possible to splice and recombine genes from one organism into the genome of another. EC 3.21.1.	Restriction Endonucleases,DNA Restriction Enzyme,Restriction Endonuclease,Endonuclease, Restriction,Endonucleases, Restriction,Enzymes, DNA Restriction,Restriction Enzyme, DNA,Restriction Enzymes, DNA
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D001483	Base Sequence	The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.	DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D015245	Deoxyribonuclease BamHI	One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/GATCC at the slash. BamHI is from Bacillus amyloliquefaciens N. Numerous isoschizomers have been identified. EC 3.1.21.-.	DNA Restriction Enzyme BamHI,Deoxyribonuclease BstI,Endonuclease BamHI,AacI Endonuclease,AaeI Endonuclease,AccEBI Endonuclease,AliI Endonuclease,ApaCI Endonuclease,BamFI Endonuclease,BamHI Deoxyribonuclease,BamHI Endonuclease,BamI Endonuclease,BamKI Endonuclease,BamNI Endonuclease,BnaI Endonuclease,BstI Deoxyribonuclease,BstI Endonuclease,DdsI Endonuclease,Endonuclease AacI,Endonuclease AaeI,Endonuclease AccEBI,Endonuclease Ali12257I,Endonuclease Ali12258I,Endonuclease AliI,Endonuclease BamFI,Endonuclease BamKI,Endonuclease BamNI,Endonuclease BnaI,Endonuclease Bst1503,Endonuclease BstI,Endonuclease DdsI,Endonuclease GdoI,Endonuclease GinI,Endonuclease GoxI,Endonuclease MleI,Endonuclease NasBI,Endonuclease NspSAIV,Endonuclease RhsI,Endonuclease SolI,GdoI Endonuclease,GinI Endonuclease,GoxI Endonuclease,MleI Endonuclease,NasBI Endonuclease,NspSAIV Endonuclease,RhsI Endonuclease,SolI Endonuclease,Endonuclease, ApaCI,Endonuclease, SolI,SolI, Endonuclease
D015246	Deoxyribonuclease EcoRI	One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence G/AATTC at the slash. EcoRI is from E coliRY13. Several isoschizomers have been identified. EC 3.1.21.-.	DNA Restriction Enzyme EcoRI,Deoxyribonuclease SsoI,Endonuclease EcoRI,Eco RI,Eco-RI,EcoRI Endonuclease,Endodeoxyribonuclease ECoRI,Endodeoxyribonuclease HsaI,Endonuclease Eco159I,Endonuclease Eco82I,Endonuclease RsrI,Endonuclease SsoI,HsaI Endonuclease,Restriction Endonuclease RsrI