cDNA clone coding for part of a mouse H-2d major histocompatibility antigen.

Kvist, Sune; Brégégère, François; Rask, Lars; Cami, B.; Garoff, Henrik; Daniel, F; Wiman, Klas G.; Larhammar, Dan; Abastado, Jean-Pierre; Gachelin, Gabriel; Peterson, Per A.; Dobberstein, Bernhard; Kourilsky, P

doi:10.1073/pnas.78.5.2772

Cited by 66 publications

(15 citation statements)

References 37 publications

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“…The corresponding cDNAs were cloned at the PstI site of pBR322 (6). A cDNA clone positive for H-2 antigens in the mRNA-DNA hybridization/cell free protein synthesis test was first isolated (6). The 400 clones of the cDNA library were further cloned by in situ colony hybridization (11).…”

Section: Methodsmentioning

confidence: 99%

“…H-2 specific mRNAs were partially purified as described earlier (10). The corresponding cDNAs were cloned at the PstI site of pBR322 (6). A cDNA clone positive for H-2 antigens in the mRNA-DNA hybridization/cell free protein synthesis test was first isolated (6).…”

Section: Methodsmentioning

confidence: 99%

“…Materials : All materials used in the present studies have been specified in earlier publications (6,7).…”

Section: Purification Of Plasmid Dnasmentioning

confidence: 99%

“…In contrast, the H-2 like antigens are poorly polymorphic (4). In the course of experiments aimed at understanding the origin of H-2 polymorphism, we (6,7) and others (8) have prepared and characterized cDNA clones copied from gene transcripts of the H-2 multigene family (8,9). We have reported earlier the nucleotide sequences of the coding region of two such clones (7).…”

Section: Introductionmentioning

confidence: 99%

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Comparison of nucleotide sequences of mRNAs belonging to the mouse H-2 multigene family

et al. 1982

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The complete nucleotide sequences of three cDNAs coding for the C-terminal part of mouse histocompatibility (H-2) antigens, and for the 3' non coding regions of these clones have been determined. Comparison of the sequences indicates a large homology throughout the coding and non-coding regions and suggests the existence of a genetic mechanism which homogenizes nucleotide sequences among genes of the H-2 multigene family.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

“…Materials : All materials used in the present studies have been specified in earlier publications (6,7).…”

Section: Purification Of Plasmid Dnasmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Comparison of nucleotide sequences of mRNAs belonging to the mouse H-2 multigene family

et al. 1982

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“…The availability of cDNA probes for genes within the MHC will permit detailed analysis of the structure of this region and an understanding of the molecular basis of polymorphic variants important in regulation of the immune response. Recently, cDNA clones corresponding to human and mouse class I and II histocompatibility antigens were described (2)(3)(4)(5)(6)(7).…”

mentioning

confidence: 99%

Isolation of cDNA clones for the human complement protein factor B, a class III major histocompatibility complex gene product.

Woods¹,

Markham²,

Ricker³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

215

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cDNA clones corresponding to a major histocompatibility class mI antigen, the complement protein factor B, have been isolated from a human adult liver cDNA library. The clones, ranging in size from 1.0 to 2.3 kilobases, were identified by direct hybridization with two synthetic oligonucleotide mixtures. Two regions of the factor B amino acid sequence, each with minimal ambiguity in codon assignment, were chosen for synthesis of the oligonucleotides. The sequences of two clones have been partially determined. They contain coding information for the amino acid sequence of the Bb fragment of factor B and the entire 3'-untranslated region.The genes for three ofthe serum complement proteins, the second (C2) and fourth (C4) components and factor B, have been localized to the major histocompatibility complex (MHC) in humans, mice, and guinea pigs (for review, see ref. 1) and have been designated class III MHC antigens. The availability of cDNA probes for genes within the MHC will permit detailed analysis of the structure of this region and an understanding of the molecular basis of polymorphic variants important in regulation of the immune response. Recently, cDNA clones corresponding to human and mouse class I and II histocompatibility antigens were described (2-7).Factor B, a single-chain serum glycoprotein (Mr, -95,000), is a component of the alternative pathway of the complement system. Activation of factor B by factor D generates two fragments, Ba (Mr, 30,000), the amino-terminal segment, and Bb (Mr =60,000). The latter fragment is associated with a cleavage product ofthe third complement (C3) component, C3b, to generate an unstable C3-cleaving enzyme (C3bBb, the C3 convertase). Factor B is an unusual serine protease, the active site of which is contained in the Bb fragment.Factor B accounts for approximately 0.1% of total protein synthesized in human liver (8). Several techniques have recently been applied to the identification of cDNA clones derived from mRNA species present in low abundance. Among these is the approach in which synthetic oligonucleotides are used indirectly as primers for cDNA synthesis and directly as probes for the detection of unique genes in Southern blot filter hybridization and colony or bacteriophage library screening (3, 9-11). By using this method, we have isolated cDNA clones for a human class III MHC antigen, factor B.METHODS mRNA Isolation and Translation and Immunoprecipitation. Fresh human adult liver was obtained from a cadaver donor (a white male, HLA A1,2; Cw3,w6; B15,w39; complotype Bf FS; C2C; C4A4,4; C4B2,QO) in accord with the Anatomical Gift Act and with the cooperation of the New England Organ Bank. Within 10 min after the tissue was obtained, it was finely minced and homogenized in 0.25 M sucrose/0.14 M NaCl/0.01 M Tris'HCI, pH 7.5/1.5 mM Mg C12 (TNMS buffer) at 00C in a glass Dounce homogenizer. The homogenate was centrifuged at 16,000 x g for 5 min at 4°C and the postmitochondrial supernatant was made 1% in NaDodSO4. Total cytoplasmic RNA was isolated by using...

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Evidence for similar function of transmembrane segments in receptor and membrane‐anchored proteins

Deber

Hsu.

et al. 1988

Biopolymers

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SynopsisTransmembrane (TM) regions of receptor proteins should have unique structural and/or chemical characteristics if these regions contain residues functional in TM signal transduction.However, in a survey of the membrane-occurring residues in 37 integral membrane proteins, we found that amino acid compositions of TM regions of receptor proteins ( n = 11) could not be distinguished statistically from corresponding regions of membrane-anchored proteins (e.g., recognition molecules) with a functional external domain attached to a single hydrophobic membranespanning anchor segment ( n = 16). TM regions in both categories of proteins differed from the compositions of TM regions in membrane-transport proteins ( n = 10). The analysis implies that TM regions in receptor proteins may function mainly to anchor (and position) receptors in their cellular membranes, and therefore residues in receptors that participate in signal transduction need not be restricted to these regions. In addition to mechanisms involving receptor aggregation, ligand-activated conformational perturbation of a receptor external aqueous domain, resulting in membrane penetration of hydrophobic segment@) of this domain to produce intramembranous contact with its cytoplasmic domain, is hypothesized as a further possible mode of signal transduction.

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cDNA clone coding for part of a mouse H-2d major histocompatibility antigen.

Cited by 66 publications

References 37 publications

Comparison of nucleotide sequences of mRNAs belonging to the mouse H-2 multigene family

Comparison of nucleotide sequences of mRNAs belonging to the mouse H-2 multigene family

Isolation of cDNA clones for the human complement protein factor B, a class III major histocompatibility complex gene product.

Evidence for similar function of transmembrane segments in receptor and membrane‐anchored proteins

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