Helen L. Barker

Rat MDC family of proteins: Sequence analysis, tissue distribution, and expression in prepubertal and adult rat testis

An increasing number of sequence‐related, cysteine‐rich membrane proteins containing metalloproteinase‐like and disintegrin‐like domains (the MDC protein family) have been identified in mammalian tissues. Here, we report the cloning and sequence analysis of cDNAs encoding several rat orthologues of this protein family, some of which are found to be expressed exclusively in the male reproductive tract, others exhibiting a broader tissue distribution. We also examine their expression in prepubertal and adult rat testis, which, in conjunction with the data on tissue distribution, form a necessary prelude to further studies aimed at establishing their individual functions. Mol. Reprod. Dev. 48:159–167, 1997.

Sequence and expression of a monkey testicular transcript encoding tMDC I, a novel member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) protein family.

Full-length clones encoding a novel member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) family of proteins have been isolated from a monkey (Macaca fascicularis) testicular cDNA library. The encoded putative 82 kDa transmembrane protein (tMDC I) shows striking sequence similarity to other members of the MDC family including rat and monkey EAP I, guinea-pig PH-30 and human MDC protein, as well as a number of snake venom components.

Genetic evidence for an additional member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) family of mammalian proteins and its abundant expression in the testis☆

Full-length clones have been isolated from a Macaca fascicularis cDNA library corresponding to a 2.65 kb mRNA present at high steady state levels in the testis. Sequence analysis suggests that the predicted translation product, tMDC II protein, represents a novel member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) family of mammalian proteins.

Isolation and characterization of α-tubulin genes from Septoria tritici and Rhynchosporium secalis, and comparative analysis of fungal α-tubulin sequences

The alpha-tubulin genes from Septoria tritici and Rhynchosporium secalis have been cloned and sequenced. The predicted amino acid sequence and intron structure showed strong homology with other known filamentous fungal alpha-tubulins. Comparison of sixteen fungal alpha-tubulin sequences based on amino acid sequence homology and intron structure identified five groups of proteins. Group 1 consists of filamentous fungi, including S. tritici and R. secalis, the dimorphic fungus Histoplasma capsulatum, and Pneumocystis carinii. Group 2 includes two divergent isoforms from Neurospora crassa and Aspergillus nidulans. Group 3 includes the yeast Saccharomyces cerevisiae and the dimorphic fungus Candida albicans. Group 4 contains the single yeast Schizosaccharomyces pombe. Group 5 includes the only Basidiomycete, Schizophyllum commune. This analysis supports the classification of P carinii as a primitive Ascomycete. The presence of an additional glycine residue between the second and third amino acid found only in Group 2 proteins may indicate a functionally distinct fungal isotype. Implications in terms of structure-function relationships for alpha-tubulin molecules are discussed.