Introns and higher-order structure in the evolution of serpins

Summary The serpins are a large family of eukaryotic proteins, many but not all of whose members are proteinase inhibitors. Most members of this family show relatively low sequence identity, but crystal structures determined for 6 different serpins are closely similar. The intron positions of 11 serpins, and the intron sizes in 9 of these 11, have been determined. There is considerable diversity in number, position, and size of introns among these serpins, though subsets show clear similarity or identity. Dendrograms derived from comparisons of DNA and amino acid sequences and of intron positions for the 11 serpins differ from each other and from dendrograms previously derived from protein sequences. These dendrograms are difficult to reconcile exclusively with a loss of introns from a large primordial set during the evolution of the serpin family. The tertiary structure of the serpins does support the idea that this protein family arose from an early recombination event which fused the amino and carboxyl domains. The structure of the carboxyl domain also suggests that an insertion subsequent to the fusion event contributed two strands of -sheet, which complemented three -sheet strands of the amino domain, to complete -sheet A, which is the central secondary structure feature of the serpins. Few of the introns lie between regions of secondary or tertiary structure, and it seems more likely that many were acquired subsequent to the early events of serpin evolution and have undergone multiple insertions, deletions, and migrations since, subject to the constraint of the serpin structure.Abbreviations Api -1-proteinase inhibitor (human) - Aci -1-antichymotrypsin (human) - Agt angiotensinogen (rat) - Oah ovalbumin (chicken) - Gyh gene y (chicken) - At3 antithrombin 3 (human) - Pi1 plasminogen activator inhibitor 1—endothelial (human) - Pi2 plasminogen activator inhibitor 2—placental (human) - Cli Cl inhibitor (human) - Apl antiplasmin (human) - Bz4 Z protein (barley).     

Coexisting mangrove-coral habitat use by reef fishes in the Caribbean

We conducted visual fish surveys in coexisting mangrove-coral (CMC) habitats in Panama to analyze the effect of coral presence in mangrove habitats on the fish assemblage. Our study revealed that CMC habitats harbor distinct fish assemblages compared to mangrove habitats without coral, with greater species richness and increased herbivore abundance. Abstract in Spanish is available with online material.     

THE EVOLUTIONARY HISTORY OF PARTHENOGENETIC CNEMIDOPHORUS LEMNISCATUS (SAURIA: TEIIDAE). II. MATERNAL ORIGIN AND AGE INFERRED FROM MITOCHONDRIAL DNA ANALYSES

Restriction endonuclease analyses were performed on mitochondrial DNAs (mtDNAs) representing unisexual parthenogenetic (cytotypes A, B, and C) and bisexual (cytotypes D and E) populations of Amazonian lizards presently regarded as Cnemidophorus lemniscatus. The results of mtDNA cleavage map comparisons among these C. lemniscatus indicated that (1) there was no cleavage site variation among the unisexuals, (2) mtDNAs from the bisexual cytotypes D and E differed in sequence from one another by about 13%, and (3) mtDNAs from cytotypes A–C differed from those of cytotype D by about 5% and from those of cytotype E by about 13%. Higher resolution restriction fragment size comparisons confirmed the high degree of similarity among the unisexual mtDNAs, but identified 12 cleavage site variants among the 13 cytotype D mtDNAs examined. Both cladistic and phenetic (UPGMA) analyses of the data indicate that the unisexual and cytotype D mtDNAs form a single clade, suggesting that a female of cytotype D was the maternal progenitor of the unisexuals. The similarity among the unisexual mtDNAs and the variability among those of cytotype D suggest that the three unisexual cytotypes arose recently from a common maternal lineage. The mtDNA variability observed among cytotype D individuals has a strong geographic component, suggesting that the unisexuals arose from one or a few geographically proximal populations. The mtDNA comparisons also support the conclusion, based on allozyme comparisons (Sites et al., 1990, this issue), that cytotypes D and E, although presently allocated to C. lemniscatus, are separate species.     

Analysis of the proposed Fe-SX binding region of Photosystem 1 by site directed mutation of PsaA in Chlamydomonas reinhardtii

The psaA and psaB genes of the chloroplast genome in oxygenic photosynthetic organisms code for the major peptides of the Photosystem 1 reaction center. A heterodimer of the two polypeptides PsaA and PsaB is thought to bind the reaction center chlorophyll, P700, and the early electron acceptors A₀, A₁ and Fe-S_X. Fe-S_X is a 4Fe4S center requiring 4 cysteine residues as ligands from the protein. As PsaA and PsaB have only three and two conserved cysteine residues respectively, it has been proposed by several groups that Fe-S_X is an unusual inter-peptide center liganded by two cysteines from each peptide. This hypothesis has been tested by site directed mutagenesis of PsaA residue C575 and the adjacent D576. The C575D mutant does not assemble Photosystem 1. The C575H mutant contains a photoxidisable chlorophyll with EPR properties of P700, but no other Photosystem 1 function has been detected. The D576L mutant assembles a modified Photosystem 1 in which the EPR properties of the Fe-S_A/B centers are altered. The results confirm the importance of the conserved cysteine motif region in Photosystem 1 structure.Dedicated to the memory of Daniel I. Arnon.