I need to write about this article, but I\'m having a bit of trouble understandi
ID: 268747 • Letter: I
Question
I need to write about this article, but I'm having a bit of trouble understanding what this paper is trying to show and how the resulting data relates to it? A simple explanation would be helpful
letters to nature 1. ina NGe,A th misochonrialprinirtmachiaur Nathur Ra SMl disorder. Thus, two functional cof FOXP2 seem to be | 339-549 (200 required for acquisition of normal spoken language. We sequenced the complementary DNAs that encode the FOXP2 15. ukauk & Han ch A 1 The H?70 a d H penchap ac ma hina Cal 351-346(1996). protein in the chimpanzee, gorilla, orang-utan, rhesus macaque and mouse, and compared them with the human cDNA. We also bminngnvestigated intraspecific variation of the human FOXP2 gene. isolation fro an Albs patient and inoculation into athyamic mics. Parasisolegy 11, 43-154 Here we show that human FOXP2 contains changes in amino- acid coding and a pattern of nudeotide polymorphism, which strongly suggest that this gene has been the target of selection in iroa-fur dusn protcin ambl Ha Mol. Cet 0, 24863-3458 (2001 during recent h umane FOXP2 (forkhead box P2) is located on human chromosome arienc a common origis for both organcles ERO21,372-579 (2002 7431, andits major splice form encodes a protein of 715 amino acids t contains 1Dyall, SD&Johron;,P.1.Origins of hydogmosors and mitochondriac volution and argancl biogenesis Curr Opin. Micahiol. , 404411 12000). belonging to the forkhead class of tr a glutamine rich regon consisting of two adi cent polyglutamine tracts, encoded by mixtures of CAG and CAA repeats. Such repeats are known to have elevated mutation rates. In the case of FOXP2 22.Tanath Fidar,A. & Clak,? Th‘nt cms,?? dargn ??? laadt mncho drainthe CnningE. in Haook of Pratactina (ds Margali LC D1)33-72 Jones and Bartlatt, Baston19 .O,lM.& Chapmanthe lengths of the polyglutamine stretches differed for all taxa studied. Variation in the second polyglutamine tract has beern impairment, but this did not co-segregate with disorder, suggesting that minor changes in length may not significantly alter the function of the protein'. If the polyglutamine stretches are disregarded, the differs at only three amino-acid positions dneh may not significantly alter theed the Chnay, A, Lafrandsbidan N l & Catany, U. Scruk gcd difinam ation of mica ponds human FOXP2 protein x. Wilbunia, S in Gaiddbook so the Malecalar Chaperosa and Protcia-Bolding Cabalysts (od. Gathing.from its orthologue in the mouse (Fig. 1). When compared witha collection of 1,880 human-rodent gene pairs, FOXP2 is among the 5% most-conserved proteins. The chimpanzee, gorilla and rhesus s are all identical to each other and carry only one difference from the mouse and two differences from the orang-utan carries two differences ihr Malalar Chpousa ad honrolling dad-an macaque FOXP2 p protein, whereas the We thank E. Canning fr the hormis culture Mem and advice on growing microsporidia: M. Duchen and A. Ball for hdp wih confocal micThomson for from the mouse and three from humans (Fig. ). Thus, although help with d aron microscopy; and C Dan ure and G.Birdey for comments on the the FOXP2 protein is highly conserved, two of the three amino acid manuscript andbe with heterologous translection experiments.IM.L aupported by differences between humans and mice occurred on the human Trust Reearch Leave Fedlowbip and Tenovus supported by a Welcome Trust Biodiversity studentship, R.P.H. was supported by a Welcome Trust University award lineage after the separation from the common ancestor with the chimpanzee. These two amino-acid differences are both found in exon 7 of the FOXP2 gene and are a t 303 and 325, respectively. Figure 2 shows the amino-acid changes, as well as the silent changes, Competing interests statement The authors declare that thay have no competing facil interat Corrapondence and requcts fir materiala should be addiewd to ?.?.?. e-mail tmhmThe u y of the relevant primates. compared the FOXP2 of T. hmnas maH0 ha bom depouited in GenBanikvariety of methods" fo humans, chimpanzees orang-utans and mice. Whereas the chimpanzee and mouse structures were essen- tially identical and the orang-utan showed only a minor change in structure, the creates a potential target site for phosphorylation by protein kinase Molecular evolution of FOXP2, a gene several studies have shown that phosphorylation of forkhead involved in speech and language tramscriptional regulation Thus lough the FoXP2 protn i C together with a minor change in predicted secondary structure. extremely conserved among mammals, it Wolfgang Enard, Molly Przeworski,Simon E. Fishert, Cecilia S.LL changes on the human lineage, at least one of which may have Victor Wiebe, Takashl Kitano, Anthony P. Monacot&Svante; Pääbo functional consequences. This is an intriguing finding, because Max Planck Institute for Evolutionary Anthropology, Inselstrasse 22, D-04108 Leipzig, Germany Wellcome Trust Centre for Human Genetics, niversity of Cacfond Roosevdlt Drive, Oxford OX3 7BN, UK Length oovaddoub? stranded, ali did Divergance from tha chimp sequance Language is a uniquely human trait likely to have been a o of varilable positions prerequisite for the development of human culture. The ability quancy 1 and 30 to develop articulate speech relies on capabilities, such as ne (nudeatide dvesty based onth ? no control of the larynx and mouth, that are absent in chimpanzees polymorphic stes) and other great apes. FOXP2 is the first gene relevant to the (lootide diversity with mone human ability to develop language. A point mutation in FOXP2 lales at high frequanay" co-segregates with a disorder in a family in which half of the ?(pExplanation / Answer
Since FOXP2 gene is involved in development of speech and language and both copies of this gene are essential to have normal speech, Point mutation in this gene leads to defects in grammatical and linguistics.
This gene has been found to show divergence among different taxa that are observed and found to contain differences in the polygluatamine stretches but minor changes does not lead to any change in terms of function.
fig1 amino acid sequence alignment data of all FOXP from different taxa are shown here, highlighted regions indiacted the forked head domain and polyglutamine stretches , the resions which are different in gorlla ,chimps, orangutan upon comparison with human indiactes that this residue might be responsible for the development of speech and language in humans as compared to others, since the protein is present in all the taxa (given), but this residue is only present within human lineage. The amino acid substitution present in exon 7 of this gene (1 or both) might have lead to the developement of orofacial movement and human language.
The change in the amino acid residue( from human and chimps from mouse 1 residue), 2 residue changes in human lineage.
Chimps and orangutan does not differ at any polymorphic positions compared to humans, allele fixation occurs back in 200, 000 years of human history
Conclusion in this paper the evolution of FOXP2 is traced along various taxa, to determine what lead to the evolution of speech and language in humans as compared to orangutans or chimps, and how the phylogeny is? what are the position where the changes are concentrated and how this changes has contributed a change in structure of this protein in different human lineage.
The variability may be due to selective sweep of this gene (change in any particular residue or position has provided a selective advantage to this over other), incresing the fitnees and evolutionary selected within human lineages.
The evidences for selective sweep was obtained from low frequency allels obtained more in number, when the exons 4, 5,6 of this gene was sequenced in individuals from africa, asia, australia, europe, south america.( D= -2.20), low D VALUE of FOXP2 compared to other human gene locii( sequenced and compared 313 humn genes.
whether this gene is showin polymorphism with different human populations or not?
Phylogenetic tree is constructed using the data showing nucleotide and amino acid changes.