Hannelore Kremling
University of Göttingen
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Featured researches published by Hannelore Kremling.
Cytogenetic and Genome Research | 1992
Wolfgang Engel; Sabine Keime; Hannelore Kremling; Horst Hameister; Gregor Schlüter
The genes for two protamines (PRM1 and PRM2) and for two transition proteins (TNP1 and TNP2) have been characterized in several mammalian species. In the human, boar, and bull, the genes for PRM1, PRM2, and TNP2 are closely linked over a stretch of DNA 13-15 kb long. Although similar data are not yet available for the mouse and rat, our results suggest that the three genes are similarly linked in these species. The gene for TNP1 in all species studied is located on another chromosome.
Cytogenetic and Genome Research | 1991
Ibrahim M. Adham; Claude Szpirer; Hannelore Kremling; S Keime; Josiane Szpirer; Göran Levan; Wolfgang Engel
The genes for proacrosin, protamines, and transition proteins are exclusively expressed in haploid spermatogenic cells. From the analysis of mouse x rat cell hybrids which segregate rat chromosomes, the rat gene for proacrosin (ACR) was assigned to chromosome 7, that for transition protein 1 (TNP1) to chromosome 9, and the genes for transition protein 2 (TNP2) and protamine 1 (PRM1) to chromosome 10.
Biochimica et Biophysica Acta | 1992
Hannelore Kremling; Notker Reinhart; Manfred Schlösser; Wolfgang Engel
Protamine 2 (PRM2) is a low molecular weight arginine-rich protein which is present in haploid spermatogenic cells of human and mouse. Although the bull PRM2 gene is translated and transcribed at low levels, the protein could not be detected. The gene was isolated from a cosmid library and was found to consist of two exons (298 and 50 bp, respectively) interrupted by an intron of 142 bp. As compared to the PRM2 genes of man, mouse and rat the bovine gene lacks a highly conserved sequence coding for the amino acids RLHRIH. Furthermore, primer extension experiments on bull PRM2 mRNA and sequencing of junction fragments revealed alternative splicing of mRNA resulting in two putative isoforms of the protein. The most abundant transcript is spliced at the conserved splice donor site found in exon 1 at position 236 giving rise to an in-frame deletion of 63 bp as compared to the cDNA sequence (Maier et al. (1990) Nucleic Acids Res. 18, 1249-1254). The less abundant longer mRNA was not detectable by radioactive primer extension. The corresponding cDNA was obtained by performing PCR with reverse transcribed bull testis RNA or with a spermatid specific cDNA library. Alternative splicing should result in an addition of 21 nonpolar amino acids in the derived polypeptide and an altered protein conformation and function.
Genomics | 1991
Hannelore Kremling; Sabine Keime; Klaus Wilhelm; Ibrahim M. Adham; Horst Hameister; Wolfgang Engel
The International Journal of Developmental Biology | 1996
Karim Nayernia; Ibrahim M. Adham; Hannelore Kremling; Kerstin Reim; Mike Schlicker; Gregor Schlüter; Wolfgang Engel
Genomics | 1992
Gregor Schlüter; Hannelore Kremling; Wolfgang Engel
Differentiation | 1989
Hannelore Kremling; Hartmut Luerssen; Ibrahim M. Adham; Uwe Klemm; Sofia Tsaousidou; Wolfgang Engel
DNA and Cell Biology | 1996
Ibrahim M. Adham; Dirk Tessmann; Khalid A. Soliman; Derek Murphy; Hannelore Kremling; Claude Szpirer; Wolfgang Engel
Biological chemistry Hoppe-Seyler | 1991
Notker Reinhart; Hannelore Kremling; Hartmut Luerssen; Ibrahim M. Adham; Wolfgang Engel
Biological chemistry Hoppe-Seyler | 1996
Ibrahim M. Adham; Hannelore Kremling; Nieter S; Zimmermann S; Hummel M; Schroeter U; Wolfgang Engel