G.S. Monastyrskaya

Pig kidney Na+,K+-ATPase: Primary structure and spatial organization

(Na+ + K+)‐ATPase α‐Subunit β‐Subunit cDNA nucleotide sequence Primary structure Glycopeptide Transmembrane arrangement

RNA polymerase rifampicin resistance mutations in Escherichia coli: Sequence changes and dominance

SummaryFive recombinant plasmids, pBK2646, pBK611, pRC3, pRC4 and pRC5, carrying rpoB rifampicin-resistant RNA-polymerase genes were obtained.The sequence analysis of these plasmids revealed certain structural changes in the rpoB gene which specify corresponding alterations in the β-subunit of RNA polymerase. Some functional properties of the corresponding mutant strains and their RNA polymerases have been investigated.

Differences in gene expression levels between early and later stages of human lung development are opposite to those between normal lung tissue and non-small lung cell carcinoma

We, for the first time, directly compared gene expression profiles in human non-small cell lung carcinomas (NSCLCs) and in human fetal lung development. Previously reported correlations of gene expression profiles between lung cancer and lung development, deduced from matching data on mouse development and human cancer, have brought important information, but suffered from different timing of mouse and human gene expression during fetal development and fundamental differences in tumorigenesis in mice and humans. We used the suppression subtractive hybridization technique to subtract cDNAs prepared from human fetal lung samples at weeks 10-12 and 22-24 and obtained a cDNA library enriched in the transcripts more abundant at the later stage. cDNAs sequencing and RT-PCR analysis of RNAs from human fetal and adult lungs revealed 12 differentially transcribed genes: ADH1B, AQP1, FOLR1, SLC34A2, CAV1, INMT, TXNIP, TPM4, ICAM-1, HLA-DRA, EFNA1 and HLA-E. Most of these genes were found up-regulated in mice and rats at later stages than in human lung development. In surgical samples of NSCLC, these genes were down-regulated as compared to surrounding normal tissues and normal lungs, thus demonstrating opposite expression profiles for the genes up-regulated during fetal lung development.

Family of human Na+,K+‐ATPase genes Structure of the gene for the catalytic subunit (αIII‐form) and its relationship with structural features of the protein

The primary structure of a gene of the Na+,K+‐ATPase multigenic family in the human genome has been determined. The gene corresponds to a hypothetical αIII‐form of the enzyme catalytic subunit. The gene comprises over 25000 bp, and its protein coding region includes 23 exons and 22 introns. Possible correlation between structural features of the protein and location of introns in the gene are discussed.

The family of human Na+K+‐ATPase genes

The multigene family of human Na,K-ATPase is composed of 5 alpha-subunit genes, 3 of which were shown to encode the functionally active alpha 1, alpha 2 and alpha 3 isoforms of the catalytic subunits. This report describes the isolation, mapping and partial sequencing of the fourth gene (ATP1AL1) that was demonstrated here to be functionally active and expressed in human brain and kidney. Limited DNA sequencing of the ATP1AL1 exons allowed one to suggest that the gene probably encodes a new ion transport ATPase rather than an isoform of the Na,K-ATPase or the closely related H,K-ATPase.

Primary structure of Escherichia coli RNA polymerase nucleotide substitution in the beta subunit gene of the rifampicin resistant rpoB255 mutant.

SummaryThe transducing phage λ dsupM814 and the plasmid pIB1830 containing the wild-type rpoB gene have been constructed and the primary structure of the genes central fragment has been established. In contrast with the wild-type, the gene of the rpoB255 mutant, whose primary structure has been published, was found to contain an A.T.→T.A. transversion entailing the substitution of a valine residue for the aspartic acid residue (516) of the wild-type β subunit.

The family of human Na,K-ATPase genesATP1AL1 gene is transcriptionally competent and probably encodes the related ion transport ATPase

The multigene family of human Na,K‐ATPase is composed of 5 α‐subunit genes, 3 of which were shown to encode the functionally active α1, α2 and α3 isoforms of the catalytic subunit. This report describes the isolation, mapping and partial sequencing of the fourth gene (ATP1AL1) that was demonstrated here to be functionally active and expressed in human brain and kidney. Limited DNA sequencing of theATP1AL1 exons allowed one to suggest that the gene probably encodes a new ion transport ATPase rather than an isoform of the Na,K‐ATPase or the closely related H,K‐ATPase.

Advances in Na+,K+-ATPase studies: from protein to gene and back to protein

Complete primary structures of both subunits of Na+,K+,ATPase from various sources have been established by a combination of the methods for molecular cloning and protein chemistry. The gene family homologous to the α‐subunit cDNA of animal Na+,K+‐ATPases has been found in the human genome. Some genes of this family encode the known isoforms (αI and αII) of the Na+,K+‐ATPase catalytic subunit. The proteins coded by other genes can be either new isoforms of the Na+,K+‐ATPase catalytic subunit or other ion‐transporting ATPases. Expression of the genes of this family proceeds in a tissue‐specific manner and changes during the postnatal development and neoplastic transformation. The complete exon‐intron structure of one of the genes of this family has been established. This gene codes for the form of the catalytic subunit, the existence of which has been unknown. Apparently, all the genes of the discovered family have a similar intron‐exon structure. There is certain correlation between the gene structure and the proposed domain arrangement of the α‐subunit. The results obtained have become the basis for the experiments which prove the existence of the earlier unknown αIII isoform of the Na+,K+‐ATPase catalytic subunit and have made possible the study of its function.

Primary structure of an EcoRI fragment of λimm434 DNA containing regions cI-cro of phage 434 and cII-O of phage lambda

Digestion of phage lambda imm434 DNA with restriction endonuclease EcoRI yields 7 fragments. The shortest among them (1287 bp) contains the right part of the phage 434 immunity region and the phage DNA portion proximal to it. The complete primary structure of this fragment has been determined using the chemical method of DNA sequencing. Hypothetical amino-acid sequences of proteins coded by the cro gene of phage 434 and the cII gene of phage lambda, as well as NH2-terminal amino-acid sequences of the cI protein of phage 434 and the O protein of phage lambda, have been deduced solely on the basis of the DNA sequence. The fragment studied contains also the pR and probably prm promoters and the oR operator of phage 434. The sequence coding for them differs from the respective DNA sequence of phage lambda.

Na+, K+-ATPase: Tissue-specific expression of genes coding for α-subunit in diverse human tissues

The expression of genes coding for α and αiii isoforms of Na+,K+‐ATPase α‐subunit has been studied in human kidney, brain, thyroid and liver cells. The expression was shown to be subjected to a tissue‐specific control and also depended on the developmental stage. The tissue‐specific expression of genes coding for different isoforms of the catalytic subunit of Na+,K+‐ATPase perhaps may be attributed to various functions of proteins belonging to this family.