Lab #4: Blast by Bishoy Galil
Date: 1/18/2018
1. The protein I searched for is hemoglobin, which has four chains to carry oxygen from the lungs to cells throughout the body. I was surprised that there are some plants and worms having hemoglobin. Plants build a single-chain hemoglobin to help protect sensitive nitrogen-fixing bacteria from oxygen, like the single chain myoglobin that stores oxygen in our muscle cells. Some bacteria also make simple forms of hemoglobin to help manage oxygen and other small molecules. Earthworms, however, are the champions when it comes to building huge hemoglobin molecules. They, and a few other types of invertebrate animals, build enormous complexes of hemoglobin to carry their oxygen, termed erythrocruorins.
2. The specific protein I chose is hemoglobin found in Pseudoterranova decipiens (Accession AAA29796), which is a cod worm that is commonly called sealworm. My hemoglobin protein is resulted from an unusual natural frameshift mutation that decreases antibody reactivity to an expressed nematode hemoglobin.
3. The amino sequence is:
1 mhssivlatv lfvaiasask trelcmksle hakvgtskea kqdgidlykh mfehypamkk
The first 10 amino acids names: Methionine - Histidine – Serine – Serine – Isoleucine – Valine – Leucine – Alanine – Threonine – Valine
4. Citation:
Authors Dixon,B., Walker,B., Kimmins,W. and Pohajdak,B.
Title An unusual natural frameshift mutation decreases antibody
5. Nucleotide sequence:
841 ttctggaaat tgtttgccga atatttgaac gaaaagagtc accaacattt gacagaagcc
Date: 1/18/2018
Bio 212 section AA
Winter 2018
Lab #4: Blast by Bishoy Galil
1. The protein I searched for is hemoglobin, which has four chains to carry oxygen from the lungs to cells throughout the body. I was surprised that there are some plants and worms having hemoglobin. Plants build a single-chain hemoglobin to help protect sensitive nitrogen-fixing bacteria from oxygen, like the single chain myoglobin that stores oxygen in our muscle cells. Some bacteria also make simple forms of hemoglobin to help manage oxygen and other small molecules. Earthworms, however, are the champions when it comes to building huge hemoglobin molecules. They, and a few other types of invertebrate animals, build enormous complexes of hemoglobin to carry their oxygen, termed erythrocruorins.
2. The specific protein I chose is hemoglobin found in Pseudoterranova decipiens (Accession AAA29796), which is a cod worm that is commonly called sealworm. My hemoglobin protein is resulted from an unusual natural frameshift mutation that decreases antibody reactivity to an expressed nematode hemoglobin.
3. The amino sequence is:
1 mhssivlatv lfvaiasask trelcmksle hakvgtskea kqdgidlykh mfehypamkk
61 yfkhrenytp advqkdpffi kqgqnillac hvlcatyddr etfdayvgel marherdhvk
121 vpndvwnhfw ehfieflgsk ttldeptkha wqeigkefsh eishhgrhsv rdhcmnsley
181 iaigdkehqk qngidlykhm fehyphmrka fkgrenftke dvqkdaffvn kdtrfcwpfv
241 ccdssyddep tfdyfvdalm drhikddihl pqeqwhefwk lfaeylneks hqhlteaekh
301 awstigedfa headkhakae kdhhegehke ehh
The first 10 amino acids names: Methionine - Histidine – Serine – Serine – Isoleucine – Valine – Leucine – Alanine – Threonine – Valine
4. Citation:
Authors Dixon,B., Walker,B., Kimmins,W. and Pohajdak,B.
Title An unusual natural frameshift mutation decreases antibody
reactivity to an expressed nematode hemoglobin.
Journal Unpublished
5. Nucleotide sequence:
1 ggaaccatta tgcactcttc aatagttttg gccaccgtgc tctttgtagc gattgcttca
61 gcatcaaaaa cgcgagagct atgcatgaaa tcgctcgagc atgccaaggt tggcaccagc
121 aaggaggcga agcaggacgg catcgacctc tacaaacata tgttcgagca ctatccagca
181 atgaagaaat acttcaagca tcgtgaaaat tatacaccgg ccgatgtcca aaaggatccc
241 ttctttatta aacaaggtca aaatatcttg ctcgcctgtc acgttttgtg cgccacatac
301 gacgatcgtg agacattcga cgcgtacgtt ggtgagctga tggcacgaca cgagcgggac
361 catgttaaag taccgaatga tgtttggaat cacttctggg aacatttcat cgagtttctg
421 ggaagtaaga ccacgttgga cgagccaacc aagcacgcat ggcaagagat cggtaaagaa
481 ttctcacatg aaatcagcca ccacggtcga cattcggttc gcgaccattg catgaactcg
541 ttggagtata tcgcgatcgg cgataaggaa catcaaaagc agaatggcat tgacctttac
601 aagcatatgt tcgagcatta tccacatatg agaaaggcat tcaagggacg cgaaaacttc
661 acgaaagaag acgttcaaaa ggacgcattc ttcgttaaca aggacacaag attctgttgg
721 cccttcgtat gctgtgactc ctcatacgat gacgagccaa cattcgacta ttttgttgat
781 gccctaatgg atcgtcatat caaagatgat attcatctac ctcaggaaca atggcatgag
841 ttctggaaat tgtttgccga atatttgaac gaaaagagtc accaacattt gacagaagcc
841 ttctggaaat tgtttgccga atatttgaac gaaaagagtc accaacattt gacagaagcc
Hi Bsihoy,
ReplyDeleteThe fact that some plants have haemoglobin is fascinating! I always thought haemoglobin would exist in blood streams as they are used to carry oxygen. It would be interesting to find out why organisms like earthworms, will have tremendous amount of haemoglobin, is it due to their simpler organelles? I also see your protein is a result of a mutation, I wonder what reducing antibody reactivity to an nematode haemoglobin would do!
Bishoy, your post was fascinating and it was an excellent choice to look at hemoglobin. Oxygen plays such a vital role in all organisms lives so hemoglobin's ability to bind and carry it makes the proteins so useful. It is also very interesting that earthworms, of all organisms, build the most complex hemoglobin for themselves. This seems counter intuitive since an earthworm is such a small organism that would not need as much oxygen as a much larger organism. However, it seems the size of the hemoglobin molecule in an organism is not dependent on the size of the organism.
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